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CysB + H2O
?
a positive cysDNC operon transcription regulator
-
-
?
CysD + H2O
?
a subunit of the sulfate adenylyltransferase, low activity
-
-
?
GlyA + H2O
?
a protein of the MetR regulon
-
-
?
PR65/A-ssrA + H2O
?
ssrA-fusion protein
-
-
?
ThiS-YbeA + H2O
?
YbeA is a alpha/beta-knot methyltransferase from Escherichia coli and a deeply 31-knotted protein. Knotted fusion protein ThiS-YbeA is degraded by ClpXP. Process modeling, overview
-
-
?
ThiS-YbeA-ssrA + H2O
?
low activity, process modeling, overview
-
-
?
UCH-L1-ssrA + H2O
?
ssrA-fusion protein, UCH-L1 is a 52-knotted protein, high activity. In degradation of UCH-L1-ssrA, the degron is located at the C-terminus of the knotted protein. C-terminally tagged UCH-L1-ssrA is not noticeably degraded by ClpXP, while N-terminally tagged ssrA-x-UCH-L1 is degraded by ClpXP. The fact that the C-terminal ssrA-tag is attached directly to beta-strand 6, which is located at the centre of the core beta-sheet structure, may explain the resistance of UCH-L1-ssrA to ClpXP-induced degradation. Mutant UCH-L1-ssrA F162A is stabilised by the mutation, mutant UCH-L1-ssrA F165A is very destabilised
-
-
?
YbeA-ssrA + H2O
?
YbeA is a alpha/beta-knot methyltransferase from Escherichia coli and a deeply 31-knotted protein. Dimeric YbeA-ssrA (ssrA-tagged fusion protein of YbeA) is degraded rapidly by ClpXP, the rate of ATP-hydrolysis by ClpXP is moderately stimulated during the degradation process. Process modeling, overview
-
-
?
Abnormal puromucyl peptides + H2O
?
-
not in vitro
-
-
?
acid resistance regulator GdE protein + H2O
?
-
degradation of GadE protein by Lon rapidly terminates the acid resistance response upon shift back to neutral pH and avoids overexpression of acid resistance genes in stationary phases
-
-
?
alpha-casein + H2O
?
-
-
-
-
?
alpha-methyl casein + H2O
?
-
-
-
?
ATP + H2O
phosphate + ADP
bacteriophage lambda N protein + H2O
?
-
-
-
-
?
Bacteriophage lambda N-protein + H2O
?
-
-
-
-
?
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
beta-casein + H2O
?
-
-
-
-
?
beta-galactosidase fragment 3-93 + H2O
?
-
a 48-residue N-terminal variant and a 33-residue C-terminal variant of beta-galactosidase fragment are degraded very slowly. Lon rapidly degrades a variant containing the 68 N-terminal residues and a variant containing the C-terminal 43 residues of the 3-93 fragment. Residues 49-68, QLRSLNGEWRFAWFPAPEAV play an important role in regocnition by Lon
-
-
?
beta-galactosidase-93-titinI27 + H2O
?
-
-
-
-
?
Canavanine-containing proteins + H2O
?
-
not in vitro
-
-
?
casein + H2O
hydrolyzed casein
CNBr-fragments of bovine serum albumin + H2O
?
-
less dependent on ATP hydrolysis
-
-
?
CspD + H2O
?
-
CspD is a replication inhibitor, which is induced in stationary phase or upon carbon starvation and increases the production of persister cells. CspD is subject to proteolysis by the Lon protease both in vivo and in vitro. Turnover of CspD by Lon is strictly adjusted to the growth rate and growth phase of Escherichia coli, reflecting the necessity to control CspD levels according to the physiological conditions. Truncation or point mutation of CspD does not elevate protein stability
-
-
?
Denatured albumin + H2O
?
-
-
-
-
?
Denatured bovine serum albumin + H2O
?
-
-
-
-
?
Denatured immunoglobulin G + H2O
?
-
-
-
-
?
Denatured lambda Cro protein + H2O
?
-
poor substrate, inhibits casein hydrolysis
-
-
?
DNA
?
-
DNA-binding site of lon is the ATPase domain
-
-
?
DNA-binding protein HUbeta + H2O
?
-
Lon binds to both histone-like proteins HUalpha and HUbeta, but selectively degrades only HUbeta in the presence of ATP. Preferred cleavage site is the A20-A21, followed in preference by L36-K37. Degradation of substrate mutants A20D and A20Q is more slowly. Mechanism follows at least three stages: binding of Lon with the HU protein, hydrolysis of ATP by Lon to provide energy to loosen the binding to the HU protein and to allow an induced-fit conformational change, and specific cleavage of only HUbeta
-
-
?
EYLFRHSDNELLHWM + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
F-QLRSLNGEWRFAWFPAPEAV-Q + H2O
F-QLRSLNG + EWRFAWFPAPEAV-Q
-
residues 4968 of betqa-galactosidase flanked by a fluorophore-quencher pair
-
-
?
FAKYWQAFRQYPRLQ + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
fluorogenic peptide S3 + H2O
?
-
-
-
?
Fluorogenic peptides + H2O
?
-
-
-
-
?
FRQYPRLQGGFVWDW + H2O
?
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
FVWDWVDQSLIKYDE + H2O
?
-
very slow degradation
-
-
?
GFP-titinI27-sul20C + H2O
?
-
when degradation initiated at the N-terminus, the full-length substrate disappears about 10fold more rapidly than when degradation initiated at the C-terminus
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
heat shock sigma factor 32 + H2O
?
-
degraded by synergistic action of lon, Clp and HflB
-
-
?
homoserine trans-succinylase + H2O
?
-
degraded by synergistic action of lon, ClpYQ, ClpXP and/or ClpAP
-
-
?
HQWRGDFQFNISRYS + H2O
?
-
degraded at rates within 30% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
human alphaA-crystallin + H2O
?
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
human alphaB-crystallin + H2O
?
-
Lon recognizes conserved determinants in the folded alpha-crystallin domain itself
-
-
?
human titin + H2O
?
-
-
-
-
?
HYPNHPLWYTLCDRY + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
IbpA + H2O
?
-
i.e. Escherichia coli small heat shock protein A. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity. IbpB stimulates Lon degradation of IbpA both in vitro and in vivo. The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation
-
-
?
IbpB + H2O
?
-
i.e. Escherichia coli small heat shock protein B. Lon degrades purified IbpA substantially more slowly than purified IbpB, which is a consequence of differences in maximal Lon degradation rates and not in substrate affinity.The variable N- and C-terminal tails of the Ibps contain critical determinants that control the maximal rate of Lon degradation
-
-
?
lambda phage N protein + H2O
?
LLIRGVNRHEHHPLH + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
LRAGENRLAVMVLRW + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
LTEAKHQQQFFQFRL + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
maltose-binding protein-SulA + H2O
?
-
-
-
-
?
MazE antitoxin + H2O
?
-
-
-
-
?
Methylglobin + H2O
?
-
methyl-apohemoglobin
-
-
?
Mutant form of alkaline phosphatase PhoA61 + H2O
?
-
not in vitro
-
-
?
MWRMSGIFRDVSLLH + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
N-glutaryl-alanylalanylphenylalanyl-3-methoxynaphthylamide + H2O
?
-
fluorogenic petide
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
Pancreatic polypeptide + H2O
?
-
-
-
-
?
Parathyroid hormone + H2O
?
-
-
-
-
?
Pro-His-Pro-Phe-His-Leu-Leu-Val-Tyr + H2O
?
-
nonapeptide related to equine angiotensinogen
-
-
?
Proteins with highly abnormal conformation + H2O
?
QLRSLNGEWRFAWFPAPEAV + H2O
QLRSLNG + EWRFAWFPAPEAV
-
variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines and fused with residues 49-68 of beta-galactosidase fragment 3-93
-
-
?
RelB antitoxin + H2O
?
-
-
-
-
?
ribosomal L13 protein + H2O
?
-
-
-
-
?
ribosomal L9 protein + H2O
?
-
-
-
-
?
ribosomal S2 protein + H2O
?
RMVQRDRNHPSVIIW + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWDLPLSDMYTPYVF + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWLPAMSERVTRMVQ + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
RWQFNRQSGFLSQMW + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
S1 peptide + H2O
?
-
decapeptide S1 containing the amino acid residues 89-98 of the bacteriophage lambdaN transcription anti-termination factor, and a fluorescence donor-acceptor pair
-
-
?
Suc-Phe-Leu-Phe-SBzl + H2O
?
-
a N-substituted tripeptide substrate
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
titin-I27CD + H2O
?
-
variant of the I27 domain of human titin containing aspartic acids in place of both wild-type cysteines
-
-
?
titinI27-beta-galactosidase-93 + H2O
?
-
-
-
-
?
titinI27-beta-galactosidase-93-titinI27 + H2O
?
-
-
-
-
?
tmRNA-tagged protein + H2O
?
transcription activator SoxS + H2O
?
-
fusion of the C-terminal domain of Rob, which is a transcription activator of the SoxRS/MarA/Rob regulon, to SoxS protects its N-terminus from Lon protease, as Lon's normally rapid degradation of SoxS is blocked in the chimera
-
-
?
Unfolded polypeptides + H2O
short peptides of 5-15 amino acids
-
broad specificity
-
?
YLEDQDMWRMSGIFR + H2O
?
-
degraded at rates within 50% of the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
YRGITCSGRQK(benzoic acid amide) + H2O
?
-
-
-
-
?
YRGITCSGRQK(benzoic acid) + H2O
?
-
S2 peptide
-
-
?
YRGITCSGRQK-(dansyl) + H2O
?
-
S4 peptide
-
-
?
YWQAFRQYPRLQGGF + H2O
?
-
degraded considerably faster than the F-QLRSLNGEWRFAWFPAPEAV-Q peptide
-
-
?
additional information
?
-
beta-casein + H2O
?
-
-
-
?
beta-casein + H2O
?
-
-
-
-
?
beta-casein + H2O
?
-
-
-
?
MetR + H2O
?
a protein of the MetR regulon
-
-
?
MetR + H2O
?
a protein of the MetR regulon, transcriptional regulator of metE expression
-
-
?
SulA + H2O
?
-
-
-
?
SulA + H2O
?
a cell division inhibitor
-
-
?
SulA + H2O
?
-
a cell division inhibitor
-
-
?
apoTorA + H2O
?
-
a molybdoenzyme; immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation
-
-
?
apoTorA + H2O
?
-
a molybdoenzyme, immature TorA (apoTorA) is degraded in vivo and in vitro by the Lon protease. Enzyme Lon interacts with apoTorA but not with holoTorA. Enzyme Lon and TorD, the specific chaperone of TorA, compete for apoTorA binding, but TorD binding protects apoTorA against degradation
-
-
?
ATP + H2O
phosphate + ADP
-
-
-
-
?
ATP + H2O
phosphate + ADP
-
high-affinity sites hydrolyze ATP very slowly, but support multiple rounds of peptide hydrolysis, while the low-affinity sites hydrolyze ATP quickly. Affinities of sites differ from one another 10fold. Hydrolysis at both the high- and low-affinity sites are necessary for optimal peptide cleavage and the stabilization of the conformational change associated with nucleotide binding
-
-
?
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
-
-
-
-
?
Bacteriophage lambda protein N + H2O
Hydrolyzed bacteriophage lambda protein N
-
cleavage sites: Ala16-Gln, Ala-Glu, Ala-Lys, Leu-Asn, Leu-Glu, Ser-Lys, Cys-Ser
-
?
casein + H2O
?
-
-
-
?
casein + H2O
?
-
lon contains three distinct domains, an amino-terminal domain having an undefined function, a central ATPase domain crucial for substrate binding and unfolding, and a C-terminal peptidase domain
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
alpha-casein
-
-
?
casein + H2O
hydrolyzed casein
-
methylcasein
-
-
?
casein + H2O
hydrolyzed casein
-
beta-casein
-
-
?
casein + H2O
hydrolyzed casein
-
guanidinated casein
-
-
?
casein + H2O
hydrolyzed casein
-
methylated alpha-casein
-
-
?
CcdA + H2O
?
-
-
-
-
?
CcdA + H2O
?
-
72-amino acid protein
-
?
Globin + H2O
?
-
-
-
-
?
Globin + H2O
?
-
beta-globin
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
-
-
-
?
Glucagon + H2O
Hydrolyzed glucagon
-
cleavage sites: Leu6-Cys(SO3H), Leu17-Val, Ala14-Leu, Val18-Cys(SO3H)
-
?
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
?
Glutaryl-Ala-Ala-Ala-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Ala + methoxynaphthylamine
-
hydrolyzed at 3-4% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
-
-
-
?
Glutaryl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Glutaryl-Ala-Ala-Phe + methoxynaphthylamine
-
fluorogenic peptide, 0.3 mM
-
-
?
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
?
Glutaryl-Gly-Gly-Pro-methoxynaphthylamide + H2O
Glutaryl-Gly-Gly-Pro + methoxynaphthylamine
-
hydrolyzed at 6% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
?
lambda phage N protein + H2O
?
-
-
-
?
lambda phage N protein + H2O
?
-
generation of a panel of fluorescent peptides based on the cleavage profile of substrate lambda phage N protein indicates that protease Lon recognizes numerous discontinouos substrate determinants throughout lambda N protein to achieve substrate promiscuity
-
-
?
mDHFR protein + H2O
?
-
sul20C-tagged protein, degradation
-
-
?
mDHFR protein + H2O
?
-
tittinI27-fusion and sul20C-tagged protein, to direct Lon degradation of a titinI27 domain, either the N or C terminus of this protein is fused to amino acids 3-93 of Escherichia coli beta-galactosidase, an unstructured sequence that contains the b20 degron, degradation
-
-
?
Melittin + H2O
?
-
-
-
-
?
Melittin + H2O
?
-
isolated proteolytic domain exhibits almost no activity toward casein, but hydrolyzes peptide substrates
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage sites
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed insulin B-chain
-
cleavage sites
-
-
?
Proteins with highly abnormal conformation + H2O
?
-
one of the heat-shock proteins under control of rpoH operon(htp R)
-
-
?
Proteins with highly abnormal conformation + H2O
?
-
rate-limiting step in breakdown of highly abnormal and some normal proteins
-
-
?
Proteins with highly abnormal conformation + H2O
?
-
catalyzes inital step in the degradation of proteins with abnormal conformation as may result from nonsense or missense mutations, biosynthetic errors or intracellular denaturation
-
-
?
RcsA + H2O
?
-
-
-
?
RcsA + H2O
?
-
protein degradation mediates the turnover of damaged proteins
-
?
ribosomal S2 protein + H2O
?
-
-
-
-
?
ribosomal S2 protein + H2O
?
-
degradation of S2 protein occurs in a processive manner. P1 and P3 sites of cleavage products are predominantly occupied by hydrophobic residues
-
-
?
ribosomal S2 protein + H2O
?
-
major lon cleavages sites within the bacterial S2 ribosomal protein located at the interior of the molecule
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
best substrate
-
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
best substrate
-
?
Succinyl-Ala-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Ala-Ala-Phe + methoxynaphthylamine
-
hydrolyzed at 137% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
-
-
?
Succinyl-Phe-Ala-Phe-methoxynaphthylamide + H2O
Succinyl-Phe-Ala-Phe + methoxynaphthylamine
-
fluorogenic peptide, hydrolyzed at 75% the rate of glutaryl-Ala-Ala-Phe-methoxynaphthylamide
-
-
?
SulA + H2O
?
-
-
-
?
SulA + H2O
?
-
physiological substrate SulA3-169 and SulA23-169
-
?
SulA + H2O
?
-
inactivation of SulA through the enzyme in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
-
-
?
tmRNA-tagged protein + H2O
?
-
-
-
-
?
tmRNA-tagged protein + H2O
?
-
highly purified lon preferentially degrades tmRNA-tagged forms of proteins compared to untagged forms
-
-
?
additional information
?
-
a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions. The recognition mechanisms of known Lon substrates are highly diverse. Misfolded proteins are mainly recognized by short, hydrophobic stretches normally buried in the core of natively folded proteins. In contrast, recognition of SulA occurs via its C-terminus with a critical histidine and tyrosine at its very end
-
-
?
additional information
?
-
-
a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions. The recognition mechanisms of known Lon substrates are highly diverse. Misfolded proteins are mainly recognized by short, hydrophobic stretches normally buried in the core of natively folded proteins. In contrast, recognition of SulA occurs via its C-terminus with a critical histidine and tyrosine at its very end
-
-
?
additional information
?
-
Escherichia coli Lon binds both single stranded DNA (ssDNA) and RNA (ssRNA), and double stranded DNA (dsDNA) in a non-specific manner, and this interaction enhances Lon ATPase and proteolytic activities
-
-
?
additional information
?
-
enzyme Ec-Lon interacts with DNA. Ec-Lon protease forms complexes with aptamers, obtained from thrombin, whose molecules comprise the duplex domains and G-quadruplex region. The aptamers have low affinities for the enzyme mutant S679A, the Lon protease does not show a strong ability to bind to any individual Gx02quadruplex (15TBA) or duplex aptamer (RE15T), but Lonx02 S679A forms complexes with twox02domain 31TBA, RE31 and ST43 aptamers
-
-
?
additional information
?
-
Lon protease has three activities: intrinsic ATPase, substrate-stimulated ATPase, and ATP-dependent proteolysis. Lon preferentially degrades damaged or misfolded proteins at its proteolytic site while the ATP is bound and hydrolyzed into ADP and phosphate at its ATPase site
-
-
?
additional information
?
-
-
Lon protease has three activities: intrinsic ATPase, substrate-stimulated ATPase, and ATP-dependent proteolysis. Lon preferentially degrades damaged or misfolded proteins at its proteolytic site while the ATP is bound and hydrolyzed into ADP and phosphate at its ATPase site
-
-
?
additional information
?
-
N-terminally truncated enzyme ClpXP can easily degrade a deeply 31-knotted and 52-knotted proteins. The degradation depends critically on the location of the degradation tag and the local stability near the tag
-
-
?
additional information
?
-
the enzyme is able to undergo autolysis and to bind DNA, analysis of formation of enzyme-DNA complexes
-
-
?
additional information
?
-
-
the enzyme is able to undergo autolysis and to bind DNA, analysis of formation of enzyme-DNA complexes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
No substrates are native bovine serum albumin, hemoglobin
-
-
?
additional information
?
-
-
No substrates are native bovine serum albumin, hemoglobin
-
-
?
additional information
?
-
-
ATP-dependent serine protease
-
-
?
additional information
?
-
-
ATP-dependent serine protease
-
-
?
additional information
?
-
-
ATP-dependent serine protease
-
-
?
additional information
?
-
-
No substrates are native albumin
-
-
?
additional information
?
-
-
No substrates are glutaryl-Phe-7-amino-4-methylcoumarin, Ala-Ala-Phe-methoxynaphthylamide, Gly-Phe-methoxynaphthylamide, Asp-methoxynaphthylamide, Leu-methoxynaphthylamide, Arg-methoxynaphthylamide, Ala-methoxynaphthylamide, Tyr-methoxynaphthylamide, Lys-methoxynaphthylamide, methoxyglutaryl-Ala-Ala-Phe-methoxynaphthylamide, methoxysuccinyl-Ala-Ala-Phe-methoxynaphthylamide, benzyloxycarbonyl-Ala-Pro-methoxynaphthylamide, benzoyl-Arg-Gly-Phe-Phe-Leu-methoxynaphthylamide, benzoyl-Arg-Gly-Leu-methoxynaphthylamide, Leu-Gly-Gly-methoxynaphthylamide, Ser-Tyr-methoxynaphthylamide
-
-
?
additional information
?
-
-
with DNA-binding ability
-
-
?
additional information
?
-
-
cleavage specificity
-
-
?
additional information
?
-
-
No substrates are lambda-repressors cI and Cro, lambda replication protein O, E. coli galactose repressor, even after heat denaturation
-
-
?
additional information
?
-
-
the active site prefers hydrophobic substrate sequences
-
-
?
additional information
?
-
-
mutant enzyme in which active site Ser-679 is replaced by Ala lacks peptidase but retains ATPase activity
-
-
?
additional information
?
-
-
no phosphorylation of enzyme or substrate during ATP hydrolysis
-
-
?
additional information
?
-
-
with a proteolytic and an ATP-binding site per monomer
-
-
?
additional information
?
-
-
No substrates are benzyloxycarbonyl-Ala-Arg-Arg-methoxynaphthylamide, native or denatured ribonuclease, native or denatured lysozyme, native immunoglobulin G
-
-
?
additional information
?
-
-
can bind to a TG-rich DNA promoter element in a sequence-specific manner
-
?
additional information
?
-
-
isolated proteolytic domain exhibits the peptidase activity
-
?
additional information
?
-
-
essential for growth of yeast on nonfermentable carbon sources
-
-
?
additional information
?
-
-
rapid proteolysis plays a major role in post-translational cellular control by the targeted degradation of short-lived regulatory proteins
-
?
additional information
?
-
-
recognition and selective degradation of abnormal and unstable proteins
-
?
additional information
?
-
-
regulation of several important cellular functions, including radiation resistance, cell division, filamentation, capsular polysaccharide production, lysogeny of certain bacteriophages, and proteolytic degradation of certain regulatory and abnormal proteins
-
?
additional information
?
-
-
enzyme and protease Clp participate in the physiological disintegration of cytoplasmic inclusion bodies, their absence minimizing the protein removal up to 40%. Clp takes the major and enzyme a minor role in processing of aggregation-prone proteins and also of polypeptides physiologically released from inclusion bodies
-
-
?
additional information
?
-
-
the polyphosphate-lon complex does not degrade intact native ribosomes
-
-
?
additional information
?
-
-
proteolytic domain and a a large N-terminal domain, active site has a Ser-Lys catalytic dyad. Proteolytic domain exhibits no detectable activity against protein substrates degraded by full-length lon, but retains a significant fraction of peptidase activity
-
-
?
additional information
?
-
-
protease Lon recognizes specific sequences rich in aromatic residues that are accessible in unfolded polypeptides but hidden in most native structures. Denatured polypeptides lacking such sequences are poor substrates. Lon also unfolds and degrades stably folded proteins with accessible recognition tags. Lon can recognize multiple signals in unfolded polypeptides synergistically, resulting in nanomolar binding and a mechanism for discriminating irreversibly damaged proteins from transiently unfolded elements of structure
-
-
?
additional information
?
-
-
enzyme recognizes degrons, i.e. degradation tags. Degron tags are also regulatory elements that determine protease activity levels. Different tags fused to the same protein change degradation speeds and energetic efficiencies by 10fold or more. Degron binding to multiple sites in the Lon hexamer differentially stabilizes specific enzyme conformations, including one with high protease and low ATPase activity, and results in positively cooperative degradation
-
-
?
additional information
?
-
-
Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible. The half-site ATPase reactivity of Lon can be used to account for the kinetic mechanism of the ATP-dependent peptidase activity of the enzyme
-
-
?
additional information
?
-
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
-
-
?
additional information
?
-
-
homooligomeric ATP-dependent LonA proteases are bifunctional enzymes
-
-
?
additional information
?
-
-
repeated cycles of ATP binding and hydrolysis power conformational changes that pull the tag through the pore and eventually tug the native portion of the substrate against the AAA+ ring, creating an unfolding force. Depending on the native substrate and enzyme, successful unfolding can require anywhere from a few to many hundreds of cycles of ATP hydrolysis
-
-
?
additional information
?
-
-
compared with hexamers, enzyme dodecamers are much less active in degrading large substrates but equally active in degrading small substrates, whcih represents a a unique gating mechanism that allows the repertoire of enzyme substrates to be tuned by its assembly state
-
-
?
additional information
?
-
-
native enzyme hydrolyzes ATP in the absence of a protein substrate
-
-
?
additional information
?
-
-
substrate specifiicty, overview. GFP-fusion proteins resist Lon degradation from the N-terminus. Partially degraded substrate fragments accumulate as proteolytic products, which is often observed during degradation in vitro of multi-domain substrates containing very stable interior domains
-
-
?
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DNA
Escherichia coli Lon binds both single stranded DNA (ssDNA) and RNA (ssRNA), and double stranded DNA (dsDNA) in a non-specific manner, and this interaction enhances Lon ATPase and proteolytic activities
Adenosine 2',3'-dialdehyde triphosphate
-
activation, hydrolysis at 23% the rate of ATP, supports proteolysis with 30% the efficiency of ATP
adenosine 5'-(3-thiotriphosphate)
Adenosine 5'-(alpha-thio)triphosphate
-
activation, Rp-diastereoisomer stimulates peptide hydrolysis much more effectively than Sp-diastereoisomer
adenosine-5'-(beta,gamma-imido)triphosphate
-
slight activation
Adenyl-5'-yl imidodiphosphate
adenyl-5'-yl methylene diphosphonate
adenyl-5'-yl methylene monophosphonate
-
i.e. AMP-CPP, activation, competes for the two ATP-high affinity sites
adenylyl 5-imidodiphosphate
-
supports peptide hydrolysis by lon
ATP
-
activates the enzyme activity
Bovine glucagon
-
activation, glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP, not casein hydrolysis
degron
-
degron binding to this site is not required for proteolysis of sul20-tagged substrates in vitro but enhances degradation by allosterically activating protease activity. Sul20 degron from the cell-division inhibitor SulA binds to the N domain of the enzyme, determination of the recognition site, overview. Allosteric role for the sul20-binding site in the N domain
-
Denatured albumin
-
activation, ATP hydrolysis
-
Denatured bovine serum albumin
-
Denatured calf thymus or E. coli DNA
-
stimulation of glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
-
Denatured immunoglobin G
-
Dimethylsulfoxide
-
activation
DNA
-
activates the enzyme activity
Polyethylene glycol
-
activation
single stranded DNA
-
ATP and protein hydrolysis
spermidine
-
activation, at physiological concentration, ATP hydrolysis and protease activity
adenosine 5'-(3-thiotriphosphate)
-
i.e. adenosine 5'-O-(thiotriphosphate) or ATP-gamma-S, activation
adenosine 5'-(3-thiotriphosphate)
-
equally effective as ATP with casein as substrate
adenosine 5'-(3-thiotriphosphate)
-
hydrolysis, peptide not protein hydrolysis
adenosine 5'-(3-thiotriphosphate)
-
not bovine serum albumin hydrolysis
adenosine 5'-(3-thiotriphosphate)
-
activates, hydrolysis of casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide
adenosine 5'-(3-thiotriphosphate)
-
slight
Adenyl-5'-yl imidodiphosphate
-
can replace ATP
Adenyl-5'-yl imidodiphosphate
-
casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
Adenyl-5'-yl imidodiphosphate
-
i.e. AMP-PNP, activation
Adenyl-5'-yl imidodiphosphate
-
competes for one of the ATP-high-affinity binding-sites
Adenyl-5'-yl imidodiphosphate
-
binding is stimulated by protein substrates
Adenyl-5'-yl imidodiphosphate
-
peptide hydrolysis
Adenyl-5'-yl imidodiphosphate
-
no activation of bovine serum albumin hydrolysis
adenyl-5'-yl methylene diphosphonate
-
i.e. AMP-PCP, activation
adenyl-5'-yl methylene diphosphonate
-
can replace ATP
adenyl-5'-yl methylene diphosphonate
-
casein or glutaryl-Ala-Ala-Phe-methoxynaphthylamide hydrolysis
casein
-
activation, glutaryl-Ala-Ala-Phe-methoxynaphthylamide or insulin B-chain hydrolysis, in the absence of ATP and synergistic with ATP
Denatured bovine serum albumin
-
activation
-
Denatured bovine serum albumin
-
glutaryl-Ala-Ala-Phe methoxynaphthylamide hydrolysis, with or without ATP
-
Denatured immunoglobin G
-
activation
-
Denatured immunoglobin G
-
peptide hydrolysis, with or without ATP
-
Globin
-
ATP hydrolysis
-
Globin
-
activation, peptide hydrolysis
-
GTP
-
activation
GTP
-
less efficient than ATP
GTP
-
hydrolysis at 113% the rate of ATP, supports proteolysis with 14% the efficiency of ATP
Polyphosphate
-
changes substrate preference of enzyme and its oligomeric structure
Polyphosphate
-
upon binding to a site in the ATPase domain, stimulation of degradation of ribosomal protein and inhibition of DNA-enzyme complex formation
Polyphosphate
-
forms a complex with lon, which enables lon to degrade free ribosomal proteins. Polyphosphate with a shorter chain length is less potent in stimulating. Polyphosphate-binding site is within the ATPase domain fo lon between amino acids 320 and 437
Polyphosphate
-
its binding within the ATPase domain of lon promotes the specific association and degradation of free ribosomal proteins
Polyphosphate
-
stimulates lon proteolytic activity, affects substrate preference and oligomeric state of the enzyme
Polyphosphate
-
stimulates lon-mediated proteolysis of free ribosomal proteins and thereby down-regulates translation
Protein substrates
-
activation
-
Protein substrates
-
promotion of ATP hydrolysis
-
Protein substrates
-
stimulation of ATP hydrolysis triggers activation of the proteolytic function
-
Protein substrates
-
rise in ATPase activity proportional to peptide bonds cleaved
-
Protein substrates
-
protein substrates, e.g. denatured bovine serum albumin induce ADP-release and promote ATP-ADP-exchange
-
Protein substrates
-
protein substrates enhance additively the stimulating effect of ATP on peptide hydrolysis and even in the absence of ATP they enhance the ability to degrade fluorogenic tripeptides
-
additional information
-
enzyme hydroylzes proteins and ATP in a coupled process
-
additional information
-
enzyme hydroylzes proteins and ATP in a coupled process
-
additional information
-
peptide substrates, e.g. glutaryl-Ala-Phe-Phe methoxynaphthylamide or succinyl-Phe-Leu-Phe methoxynaphthylamide do not support ATP hydrolysis
-
additional information
-
no activation by benzoyl-Arg-Gly-Phe-Phe-Leu methoxynaphthylamide (glutaryl-Ala-Ala-Phe methoxynaphthylamide as substrate), poly(A)
-
additional information
-
no activation by nonhydrolyzable proteins, e.g. native or denatured ribonuclease or lysozyme
-
additional information
-
polyphosphate (n:17)
-
additional information
-
nonhydrolyzable ATP-analogs are much less effective than ATP in supporting hydrolysis of large proteins
-
additional information
-
no activation by ubiquitin
-
additional information
-
no activation by ubiquitin
-
additional information
-
protein degradation requires nucleoside triphosphate hydrolysis, cleavage of small peptides only requires binding of nucleotides to the enzyme
-
additional information
-
ATP cannot be replaced by adenosine 5'-(beta-thiotriphosphate)
-
additional information
-
no activation by mRNA, tRNA, poly(rA), (dT)10
-
additional information
-
ATP cannot be replaced by ADP, AMP
-
additional information
-
ATP cannot be replaced by ADP, AMP
-
additional information
-
degradation of proteins stimulates ATPase activity of lon
-
additional information
-
lon gene is heat shock-induced
-
additional information
-
the enzyme activity of Lon can be stimulated by the presence of unfolded proteins (e.g. apomyoglobin, glucagon, and alpha-casein) as well as inorganic polyphosphate accumulated during amino acid starvation
-
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metabolism
ATP-dependent Lon protease of Escherichia coli (Ec-Lon) is a key enzyme of the quality control system of the cell proteome
malfunction
-
deletion of Lon's ATPase domain abrogates interactions with DNA. Substitution of positively charged amino acids in this domain in full-length Lon with residues conferring a net negative charge disrupts binding of Lon to DNA. These changes also affect the degradation of nucleic acid binding protein substrates of Lon, intracellular localization of Lon, and cell morphology. The DNA-binding defect of Lon protease affects plasmid replication initiator protein TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex. The phenotype of the DNA binding-defective Lon mutants is similar to that observed for Lon-deficient strains
evolution
human enzyme hLon and Escherichia coli enzyme ELon bind to ADP and undergo at least one structural change that exposes the same tryptic digestion site, suggesting the presence of at least one conserved structural change in the two enzyme homologues upon binding to ADP
evolution
Lon is a highly conserved member of the AAA+ (ATPases associated with diverse cellular activities) protease family
evolution
Lon proteases can be divided into two subfamilies: LonA (found in eubacteria and eukarya) and LonB (found in archaea). LonA proteases are formed by three functional domains: the N-terminal, involved in substrate binding, the central AAA+ domain, and the C-terminal domain (named P domain), which containing the Ser-Lys catalytic dyad for proteolytic activity. LonB proteases are composed by an ATPase and a protease domain and a hydrophobic transmembrane region which anchors the protein to the internal face of cell membrane
evolution
LonA from Escherichia coli belongs to the superfamily of AAA+ proteins, family S16 of proteases. The presence of an extended variable N-terminal region preceding the AAA+ modules is a characteristic feature of LonA proteases distinguishing them from other AAA+ proteins
evolution
the enzyme belongs to the protease family S16 and to the superfamily of AAA+ proteins
evolution
the enzyme belongs to the protease fasmily S16
malfunction
a Lon trapping variant, which is able to translocate substrates but unable to degrade them, is established and used for substrate determinations by mass spectrometry
malfunction
removal of the HI(CC) domain results in a dexadcrease in the activity of the peptidase center of the Ec-Lon protease and a loss of the regulatory effect of the ATPase center on the peptidase one, which is defined by the nature of the bound nucleotide in the intact enxadzyme. Deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form
malfunction
the deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested
malfunction
the Lon mutant variant V217A/Q220A (LonVQ) forms a dodecamer with increased stability compared to wild-type. Cells expressing only LonVQ are healthier than Lon-deficient strains during normal growth and perform similarly to wild-type Lon in a panel of in vivo bioassays except for degradation of small heat shock proteins. At 37°C, the enzyme-ddeficient DELTAlon strain grows significantly slower than the wild-type strain and never establishes a true exponential phase, but loss of Lon activity is not deleterious to viability
physiological function
a quantitative Super-SILAC (stable isotope labeling with amino acids in cell culture) mass spectrometry approach and analysis of proteomes of a lon mutant and a strain producing the protease are employed to determine substrate specificity and Lon-dependent physiological functions, Lon affected proteins, overview. Fundamental functions of Lon in sulfur assimilation, nucleotide biosynthesis, amino acid and central energy metabolism, besides the superoxide stress response function. Lon protease affects the MetR regulon and function of proteins MetE and MetR
physiological function
Lon protease is one of the main participants of the proteome quality control (PQC) system supporting normal cell homeostasis. The PQC system involves molecular chaperones participating in the remodeling and disaggregation of cellular proteins and ATP-dependent peptide hydrolases, which control the level of regulatory proteins through selective proteolysis and eliminate potentially hazardous, anomalous, defective, and redundant proteins from cells through their exhaustive degradation. All proteases of the PQC system are bifunctional enzymes whose proteolytic activity is coupled with the simultaneous ATP hydrolysis and is characterized by a processive mechanism of the hydrolysis of protein targets (without the release of high-molecular-weight intermediates)
physiological function
LonA from Escherichia coli plays a key role in the quality control system of the cell proteome. It destroys abnormal and defective polypeptides, as well as a number of regulatory proteins, according to a processive degradation mechanism
physiological function
multidomain ATP-dependent Lon protease of Escherichia coli is one of the key enzymes of the quality control system of the cellular proteome. The HI(CC) domain of Ec-Lon protease is required for the formation of a functionally active enzyme structure and for the implementation of protein-protein interactions
physiological function
the protein quality control network (pQC) plays critical roles in maintaining protein and cellular homeostasis, especially during stress. Protease Lon is one of the central proteases responsible for protein quality control (pQC). It is the principal enzyme that degrades most unfolded or damaged proteins. Degradation by Lon also controls cellular levels of several key regulatory proteins. Analysis of biological roles of the Lon dodecamer. The enzyme dodecamer successfully completes many of the Lon protease's important regulatory functions while modifying substrate choice, perhaps to better manage protein quality control under conditions such as UV, heat, and oxidative stress
physiological function
together with its proteolytic and chaperone activities, Lon ability to bind mtDNA is conserved from bacteria to mammalian mitochondria. Escherichia coli Lon binds both single stranded DNA (ssDNA) and RNA (ssRNA), and double stranded DNA (dsDNA) in a non-specific manner, and this interaction enhances Lon ATPase and proteolytic activities. Lon ability to bind to DNA needs conformational changes in Lon itself, and such changes are inhibited by ATP, and are stimulated by a protein substrate
evolution
-
evolution has diversified rather than optimized the protein unfolding activities of different AAA+ proteases, Escherichia coli utilizes five different AAA+ proteases: Lon, ClpXP, ClpAP, HslUV, and FtsH
evolution
-
homooligomeric ATP-dependent LonA proteases are bifunctional enzymes belonging to the superfamily of AAA+ proteins
physiological function
-
absence of Lon protease blocks paradoxical survival occurring at very high nalidixic acid concentrations. The absence of Lon also blocks a parallel increase in cell lysate viscosity likely to reflect DNA size
physiological function
-
Lon possesses an intrinsic ATPase activity that is stimulated by protein and certain peptide substrates. The ATPase reaction catalyzed by Lon in the presence and absence of peptide substrate that stimulates the enzyme's ATPase activity is irreversible
physiological function
-
the alpha-domain from Lon binds to the duplex nucleotide sequence 5'-CTGTTAGCGGGC-3' from pET28a plasmid DNA sequence map and protects it from DNase I digestion. The Brevibacillus thermoruber Lon alpha-domain binds with 5'-CTGTTAGCGGGC-3' double-stranded DNA tighter than Lon alpha-domains from Escherichia coli and Bacillus subtilis, whereas the Brevibacillus thermoruber Lon alpha-domain has dramatically lower affinity for double-stranded DNA with 0 and 50% identity to the 5'-CTGTTAGCGGGC-3' binding sequence
physiological function
-
the Lon protease and the SecB and DnaJ/Hsp40 chaperones are involved in the quality control of presecretory proteins in Escherichia coli. Mutations in the lon gene alleviate the cold-sensitive phenotype of a secB mutant. In comparison to the respective single mutants, the double secB lon mutant strongly accumulates aggregates of SecB substrates at physiological temperatures, suggesting that the chaperone and the protease share substrates. The main substrates identified in secB lon aggregates, namely proOmpF and proOmpC, are highly sensitive to specific degradation by Lon. In contrast, both substrates are significantly protected from Lon degradation by SecB. The chaperone DnaJ by itself protects substrates better from Lon degradation than SecB or the complete DnaK/DnaJ/GrpE chaperone machinery
physiological function
-
transposon inactivation of ycgE, encoding a putative transcriptional regulator, leads to decreased multidrug susceptibility in an Escherichia coli lon mutant. The multidrug susceptibility phenotype e.g., to tetracycline and beta-lactam antibiotics, requires the inactivation of both lon and ycgE. In this mutant, a decreased amount of OmpF porin contributes to the lowered drug susceptibility, with a greater effect at 26°C than at 37°C
physiological function
-
AAA+ proteases employ a hexameric ring that harnesses the energy of ATP binding and hydrolysis to unfold native substrates and translocate the unfolded polypeptide into an interior compartment for degradation. Ability of theLon protease to unfold and degrade model protein substrates beginning at N-terminal, C-terminal, or internal degrons, unfolding with robust and processive unfolding/degradation of some substrates with very stable protein domains, including mDHFR and titin, overview
physiological function
-
Lon is an ATPase associated with cellular activities protease that controls cell division in response to stress and also degrades misfolded and damaged proteins
physiological function
-
protease Lon eliminates an immature or misfolded molybdoenzyme probably by targeting its inactive catalytic site, it is involved in the apoTorA degradation process
physiological function
-
the ATP-dependent Lon protease is a key component of the quality control system, which ensures the integrity and functionality of cellular proteins
physiological function
-
the enzyme can function as a protease or a chaperone and reveal that some of its ATP-dependent biological activities do not require translocation. Enzyme-mediated relief of proteotoxic stress and protein aggregation in vivo can also occur without degradation but is not dependent on robust ATP hydrolysis. Degron binding regulates the activities of the AAA+ Lon protease in addition to targeting proteins for degradation, degron binding regulates Lon ATPase and protease activity in addition to serving a recognition function. Inactivation of cell-division inhibitor SulA in vivo requires binding to the N domain and robust ATP hydrolysis but does not require degradation or translocation into the proteolytic chamber
physiological function
-
Lon-DNA interactions are essential for Lon activity in cell division control. The ability of Lon to bind DNA is determined by its ATPase domain. This binding is required for processing protein substrates in nucleoprotein complexes, and Lon may help regulate DNA replication in response to growth conditions
additional information
the C-terminal part of the HI(CC) domain has an allosteric effect on the efficiency of the functioning of both ATPase and proteolytic sites of the enzyme, while the coiled-coil (CC) fragment of this domain interacts with the protein substrate. Analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for utodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
-
the C-terminal part of the HI(CC) domain has an allosteric effect on the efficiency of the functioning of both ATPase and proteolytic sites of the enzyme, while the coiled-coil (CC) fragment of this domain interacts with the protein substrate. Analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for utodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
the CC region is involved in the recognition of the nucleotide nature by the enzyme and the interaction of the enzyme with the protein substrate, effect of the coiled-coil (CC) region of the alpha-helical inserted domain of Escherichia coli Lon protease (Ec-Lon) on the functional activity of the enzyme, overview. The CC region is necessary for the formation and functioning of the ATPase and peptidase active centers, the occurrence of allosteric interactions between them, and for the implementation of proteolysis by a unique processive mechanism
additional information
the enzyme Ec-Lon is a bifunctional homohexameric enzyme, its subunit comprises an N-terminal noncatalytic region, two-domain ATPase module, and a proteolytic domain with serine-lysine endopeptidase activity
additional information
the enzyme's active site has a Ser-Lys catalytic dyad
additional information
-
the AAA+ ATPase module and protease domain of Lon are part of a single polypeptide
additional information
-
the second alpha-helical domain plays a crucial role in ATP hydrolysis and enzyme binding to the target protein, while the first alpha-helical domain is not important for the manifestation of the catalytic properties of the enzyme, but it affects the functioning of Lon ATPase and peptidase sites and is involved in maintaining enzyme stability, participation of the first alpha-helical domain in the formation of three-dimensional structures of LonA proteases and/or their complexes with DNA
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Q220C
site-directed mutagenesis, the mutant reproducibly yields fast and robust intermolecular disulfide crosslinking. The cysteine-based disulfide crosslinking is responsible for the formation of the SDS-resistant dimers
R164A
site-directed mutagenesis, mutation of a HI(CC) domain residue, helix H3, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
R192A
site-directed mutagenesis, mutation of a HI(CC) domain residue, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
V217A/Q220A
site-directed mutagenesis, residues Val217 and Gln220 are present in a region predicted to form intermolecular coiled coils between hexamers, the Lon mutant variant (LonVQ) forms a dodecamer with increased stability compared to wild-type. The dodecamer is active, but it exhibits alterations in substrate selection and/or degradation. Mutant LonVQ is altered in recognition of dodecamer-sensitive substrates in vivo
V217C
site-directed mutagenesis, the mutant reproducibly yields fast and robust intermolecular disulfide crosslinking. The cysteine-based disulfide crosslinking is responsible for the formation of the SDS-resistant dimers
Y294A
site-directed mutagenesis, mutation of a HI(CC) domain residue, the mutant shows highly reduced ATPase activity in presence of beta-casein compared to the wild-type
D743N
-
site-directed mutagenesis
E240K
-
site-directed mutagenesis
E424Q
-
site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis. The mutant translocates and degrades CM-titinI27-sul20 and CM-titinI27-beta20 at a very slow rate. The mutation stabilizes the enzyme conformation that is active in relieving stress
E424Q/S679A
-
site-directed mutagenesis, the mutant is unable to inactivate SulA in vivo and displays reduced rates of both basal and substrate-stimulated ATP hydrolysis
H665Y
-
site-directed mutagenesis
H667Y
-
site-directed mutagenesis
K362A
-
site-directed mutagenesis
K362Q
-
intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation
K371E/K376E/R379E
-
site-directed mutagenesis, mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous
R164A
-
site-directed mutagenesis, the ATPase activity of the mutant is markedly reduced compared to the wild-type enzyme, thhe mutant retains the ability to hydrolyze PepTBE in the absence of effectors
R306E/K308E/K310E/K311E
-
site-directed mutagenesis, the mutant demonstrates significantly reduced DNA binding capabilities compared to wild-type enzyme. The Lon mutant does not restore cell length in the lon-/- strain, cells remained filamentous
R542A
-
site-directed mutagenesis, the mutant completely loses its ability to hydrolyze ATP, the mutant retains the ability to hydrolyze PepTBE in the absence of effectors
T704A
-
retains significant proteolytic activity
Y398A
-
site-directed mutagenesis, the mutant has basal ATP-hydrolysis activity similar to wild-type Lon, but displays substantially reduced rates of ATP hydrolysis in the presence of sul20- or beta20-tagged substrates
S679A
interaction analysis with thrombin-derived aptamers, overview
S679A
site-directed mutagenesis, the Lon trapping variant is able to translocate substrates but unable to degrade them, it is established and used for substrate determinations by mass spectrometry
D676N
-
site-directed mutagenesis
D676N
-
is completely inactive for protein degradation, it retains some basal ATPase activity, but no activation of ATPase activity occurs upon binding of protein substrates
E614K
-
single point mutation in the gene lonR9
E614K
-
is a dominant-negative mutant, can form mixed oligomers with wild-type lon and interferes with its activity
E614K
-
mixed oligomeric complexes composed of wild-type lon and the inactive lon E614K mutant, results in an enzymatically inactive protein
S679A
-
site-directed mutagenesis
S679A
-
proteolytically inactive
S679A
-
inactive, intersubunit domain-domain interactions between ATPase and proteolytic sites by complementation
S679A
-
proteolytically inactive, but wild-type-like intrinsic and peptide-stimulated ATPase activitiy. Two-step peptide S4 binding event, where a conformational change occurs after a rapid equilibrium peptide binding step
S679A
-
complete loss of activity. Mutant is not capable of restoring the secB cold sensitive phenotype, indicating that the deleterious effect of Lon in the secB mutant is due to its protease activity
S679A
-
site-directed mutagenesis, the S679A mutation destabilizes the enzyme conformation that is active in relieving stress
S679W
-
proteolytically inactive mutant. ATPase activity is affected by a variety of mutations generated at the vicinity of the proteolytic site Ser 679. Mutation of the ATP-binding site abolishes both the ATPase and protease activities of lon
S679W
-
proteolytically inactive, but wild-type-like intrinsic and peptide-stimulated ATPase activitiy. Two-step peptide S4 binding event, where a conformational change occurs after a rapid equilibrium peptide binding step
additional information
analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for autodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
-
analysis of the propensity of C-His-Lon and mutant enzymes Lon-R164A, Lon-R192A, and Lon-Y294A for autodegradation reveals that Lon-Y294A is most prone to autolysis. Slight autolysis of the intact enzyme and the mutant forms of Lon-R164A and Lon-R192A is observed only in the absence of nucleotides
additional information
construction of a recombinant form des-CC(G5)-Lon in which the deleted CC fragment, a deleted 108-unit coiled-coil fragment (residues M173-M280) is replaced by a pentaglycine peptide, the the ClpB chaperone of Thermus thermophilus. Analysis of enzymatic properties of des-CC(G5)-Lon-H6 (DELTArLon) mutant, overview. In the absence of nucleotide effectors as well as in the presence of free nucleotides or the ADP-Mg complex, casein is not hydrolyzed by rLon even if the duration of the experiment is increased many times. The deletion form DELTArLon is incapable of hydrolyzing beta-casein in the time interval in which the proteolytic activity of full-length rLon protease is tested
additional information
construction of an N-terminally truncated ClpX lacking residues 1-62, ClpXDELTAN
additional information
removal of the HI(CC) domain, deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form. The deletion form Lon-dHI(CC) is unstable and it undergoes autolysis both in the absence and presence of nucleotide effectors, the autolysis of Lon-dHI(CC) is most pronounced in the presence of Mg2+ ions
additional information
-
removal of the HI(CC) domain, deletion of the HI(CC) domain leads to a complete loss of the proteolytic activity towards beta-casein by the deletion form. The deletion form Lon-dHI(CC) is unstable and it undergoes autolysis both in the absence and presence of nucleotide effectors, the autolysis of Lon-dHI(CC) is most pronounced in the presence of Mg2+ ions
additional information
-
overproduction of enzyme is lethal. Overproduction specifically inhibits translation through specific activation of YoeB-dependent mRNA cleavage
additional information
-
in an endogenous protein tagging assay, lon mutants accumulate excessive levels of tmRNA-tagged proteins. In a reporter protein tagging assay with lambda-CI-N, lon mutants efficiently tag the reporter protein, but the tagged protein exhibits increased stability. GFP construct containing a hard-coded C-terminal tmRNA tag exhibits increased stability in lon mutant cells
additional information
-
lon clp ppk triple mutant, rate of protein turnover ist nearly identical to that of the lon clp double mutant. Deletion mutants of lon fused to the C-terminus of maltose-binding protein
additional information
-
lon gene mutants, form long undivided filaments upon UV irradiation
additional information
-
lon mutant altered in substrate specificity. A mutation in lon that converts Glu240 to Lys results in stabilization of lon substrate RcsA in vivo but does not affect the degradation of lon substrate SulA. lon lacking 107 N-terminal residues has drastically reduced protein degrading activity in vitro
additional information
-
lon mutant, confers partial resistance against colicin. Sensitivity of lon mutant to colicin can be rescued by complementation. Decrease in the protein expression levels of BtuB and OmpF in the lon mutant, which are involved in colicin translocation. Elevation of expression of the oxyS gene, which can negatively control on the expression of BtuB protein
additional information
-
lon mutants, accumulate abnormal proteins, form mucoid colonies and long filaments, fail to adapt rapidly to a nutrional downshift, are sensitive to UV at 30°C because of SulA accumulation, at higher temperatures they lose their sensitivity because ClpYQ takes over SulA degredation
additional information
-
lon- mutants survive equally well under aerobic conditions as the wild-type, but die more rapidly than the wild-type under anaerobiosis. Effect is not mediated through a compensatory increase in the Clp protease
additional information
-
in gene disruption mutant lon::Tn10 members of the RcsA regulon and many genes of the sigmaS-dependent general stress response are upregulated. The lon mutation does not affect sigmaS levels nor sigmaS activity in general. Lon-affected genes also include the major acid resistance genes
additional information
-
the combined absence of Lon and SecB leads to a significant increase in protein aggregation at 37°C. The most abundant aggregated species are proteins destined for export. Data suggest that Lon and SecB share some substrates and that the SecB chaperone protects them from Lon degradation at both high and low temperatures
additional information
-
construction of enzyme mutants, fusion of the Lon N domain to Escherichia coli ClpXDELTAN, a AAA+ enzyme that forms stable ring hexamers. Chimera307 contained the entire Lon N domain (residues 1-307) fused to ClpXDELTAN, whereas chimera211 contains the first 211 residues of Lon, which includes a globular region of the N domain but not an extended helical region. In addition, chimera211 contains disulfide bonds between the subunits of ClpXDELTAN, which have been shown to stabilize functional covalent hexamers. The ClpXDELTAN hexamerization is required for functional interaction with ClpP
additional information
-
generation of mutant LonDELTANP lacking the ATP domain. Deletion of Lon's ATPase domain abrogates interactions with DNA. The DNA-binding defect of Lon protease affects TrfA proteolysis. And the Lon mutants are defective in proper cellular localization, most probably due to their impaired ability to form a nucleoprotein complex
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Liao, J.H.; Lin, Y.C.; Hsu, J.; Lee, A.Y.; Chen, T.A.; Hsu, C.H.; Chir, J.L.; Hua, K.F.; Wu, T.H.; Hong, L.J.; Yen, P.W.; Chiou, A.; Wu, S.H.
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Escherichia coli
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Sakr, S.; Cirinesi, A.M.; Ullers, R.S.; Schwager, F.; Georgopoulos, C.; Genevaux, P.
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Escherichia coli
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Bissonnette, S.A.; Rivera-Rivera, I.; Sauer, R.T.; Baker, T.A.
The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease
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Escherichia coli
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Gur, E.; Sauer, R.T.
Degrons in protein substrates program the speed and operating efficiency of the AAA+ Lon proteolytic machine
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Escherichia coli
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Li, M.; Gustchina, A.; Rasulova, F.S.; Melnikov, E.E.; Maurizi, M.R.; Rotanova, T.V.; Dauter, Z.; Wlodawer, A.
Structure of the N-terminal fragment of Escherichia coli Lon protease
Acta Crystallogr. Sect. D
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2010
Escherichia coli (P0A9M0), Escherichia coli
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Minami, N.; Yasuda, T.; Ishii, Y.; Fujimori, K.; Amano, F.
Regulatory role of cardiolipin in the activity of an ATP-dependent protease, Lon, from Escherichia coli
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Escherichia coli
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Langklotz, S.; Narberhaus, F.
The Escherichia coli replication inhibitor CspD is subject to growth-regulated degradation by the Lon protease
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Escherichia coli
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Redelberger, D.; Genest, O.; Arabet, D.; Mejean, V.; Ilbert, M.; Iobbi-Nivol, C.
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Escherichia coli
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Wohlever, M.L.; Baker, T.A.; Sauer, R.T.
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Escherichia coli
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Vieux, E.F.; Wohlever, M.L.; Chen, J.Z.; Sauer, R.T.; Baker, T.A.
Distinct quaternary structures of the AAA+ Lon protease control substrate degradation
Proc. Natl. Acad. Sci. USA
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Escherichia coli
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Gur, E.; Vishkautzan, M.; Sauer, R.
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Andrianova, A.; Kudzhaev, A.; Serova, O.; Dergousova, N.; Rotanova, T.
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Kudzhaev, A.; Andrianova, A.; Dubovtseva, E.; Serova, O.; Rotanova, T.
Role of the inserted alpha-helical domain in E. coli ATP-dependent lon protease function
Acta Naturae
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2017
Escherichia coli (P0A9M0), Escherichia coli
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Pinti, M.; Gibellini, L.; Nasi, M.; De Biasi, S.; Bortolotti, C.A.; Iannone, A.; Cossarizza, A.
Emerging role of Lon protease as a master regulator of mitochondrial functions
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Fishovitz, J.; Sha, Z.; Chilakala, S.; Cheng, I.; Xu, Y.; Lee, I.
Utilization of mechanistic enzymology to evaluate the significance of ADP binding to human Lon protease
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Escherichia coli (P0A9M0), Escherichia coli, Homo sapiens (P36776), Homo sapiens
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Karlowicz, A.; Wegrzyn, K.; Gross, M.; Kaczynska, D.; Ropelewska, M.; Siemiatkowska, M.; Bujnicki, J.M.; Konieczny, I.
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Escherichia coli
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Brown, B.L.; Vieux, E.F.; Kalastavadi, T.; Kim, S.; Chen, J.Z.; Baker, T.A.
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Escherichia coli (P0A9M0), Escherichia coli
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Arends, J.; Griego, M.; Thomanek, N.; Lindemann, C.; Kutscher, B.; Meyer, H.E.; Narberhaus, F.
An integrated proteomic approach uncovers novel substrates and functions of the Lon protease in Escherichia coli
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2018
Escherichia coli (P0A9M0), Escherichia coli
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Kudzhaev, A.; Andrianova, A.; Serova, O.; Arkhipova, V.; Dubovtseva, E.; Rotanova, T.
The effect of mutations in the inserted domain of ATP-dependent Lon protease from E. coli on the enzyme function
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2015
Escherichia coli (P0A9M0), Escherichia coli
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Spiridonova, V.; Kudzhaev, A.; Melnichuk, A.; Gainutdinov, A.; Andrianova, A.; Rotanova, T.
Interaction of DNA aptamers with the ATP-dependent Lon protease from Escherichia coli
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2015
Escherichia coli (P0A9M0)
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Kudzhaev, A.; Dubovtseva, E.; Serova, O.; Andrianova, A.; Rotanova, T.
Effect of the deletion of the (173-280) fragment of the inserted alpha-helical domain on the functional properties of ATP-dependent Lon protease from E. coli
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2018
Escherichia coli (P0A9M0)
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brenda
Sivertsson, E.M.; Jackson, S.E.; Itzhaki, L.S.
The AAA+ protease ClpXP can easily degrade a 31 and a 52-knotted protein
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2019
Escherichia coli (P0A9M0)
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