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D185G
dimerization, RNA binding, 7% activity compared to wild-type
D58A
dimerization, RNA binding, no activity
Deletion A252
dimerization, RNA binding, no activity
Delta200-212
weak dimerization, no RNA binding, no activity
Delta270-280
multimerization, no RNA binding, no activity
Delta49-164
weak dimerization, no RNA binding, no activity
Delta51-60
weak dimerization, no RNA binding, no activity
G184V
weak dimerization, no RNA binding, no activity
H133L
dimerization, weak RNA binding, no activity
H226L
dimerization, RNA binding, no activity
H248L
multimerization, no RNA binding, no activity
H54L
dimerization, weak RNA binding, no activity
H56L
weak dimerization, weak RNA binding, no activity
H59L
multimerization, no RNA binding, no activity
K203I
multimerization, no RNA binding, no activity
L205I
weak dimerization, RNA binding, 56% activity compared to wild-type
P83L
multimerization, no RNA binding, no activity
T186I
multimerization, no RNA binding, no activity
T210I
weak dimerization, RNA binding, 85% activity compared to wild-type
Y140L
weak dimerization, RNA binding, 30% activity compared to wild-type
Y253S
dimerization, RNA binding, 23% activity compared to wild-type
D211A
-
Asp(II), active site residue
D67A
-
Asp(I), active site residue
H140A
-
His(IV), active site residue
H247A
-
His(V), active site residue
H269A
-
His(VI), active site residue
H63A
-
His(I), active site residue
H68A
-
His(III), active site residue
A493T
processing efficiency similar to wild-type tRNase Z
A501T
processing efficiency similar to wild-type tRNase Z
A631T
HEAT-domain-variant
C442A
12fold reduction of processing efficiency compared to wild-type
C467A
8fold reduction of processing efficiency compared to wild-type
D466A
1500fold reduction of processing efficiency compared to wild-type
D502T
processing efficiency reduced 7420fold compared to wild-type tRNase Z
DELTAFA
deletion of the flexible arm (FA) hand close to its boundaries with the stalk does not interfere with stability and expression of tRNase ZL. DELTAFA hand variant has a Km ca. 100times higher and a kcat ca. 2times lower than wild-type tRNase Z
E469A
300fold reduction of processing efficiency compared to wild-type
E630A
HEAT-domain-variant
G196A/Pro201A
increases in Km as compared to wild-type tRNase Z
G200A
significant reductions in kcat as compared to wild-type tRNase Z
G209A
increases in Km as compared to wild-type tRNase Z
G438A
5000fold reduction of processing efficiency compared to wild-type
G440A
4fold reduction of processing efficiency compared to wild-type
G468A
900fold reduction of processing efficiency compared to wild-type
G470A
13fold reduction of processing efficiency compared to wild-type
G473A
8fold reduction of processing efficiency compared to wild-type
G480A
8fold reduction of processing efficiency compared to wild-type
G506A
processing efficiency reduced 11fold compared to wild-type tRNase Z
H498A
processing efficiency reduced 1950fold compared to wild-type tRNase Z
H500A
processing efficiency reduced 3379fold compared to wild-type tRNase Z
H503A
processing efficiency reduced 817fold compared to wild-type tRNase Z
H504A
processing efficiency reduced 7fold compared to wild-type tRNase Z
H629A
HEAT-domain-variant
I212A
increases in Km as compared to wild-type tRNase Z
I443A
8fold reduction of processing efficiency compared to wild-type
I475A
5fold reduction of processing efficiency compared to wild-type
I494A
processing efficiency similar to wild-type tRNase Z
I505A
processing efficiency similar to wild-type tRNase Z
I508A
processing efficiency reduced 6fold compared to wild-type tRNase Z
K214A/Lys218A
significant reductions in kcat as compared to wild-type tRNase Z
K446A
25fold reduction of processing efficiency compared to wild-type
L187A
substitution of alanine causes Km to increase almost as much as deletion of the entire flexible arm hand, with barely any decrease in kcat. A higher concentration of L187A enzyme than that of wild-type tRNase Z has to be used to accommodate the lower catalytic efficiency of the variant
L206A
increases in Km as compared to wild-type tRNase Z
L437A
7fold reduction of processing efficiency compared to wild-type
L464A
5fold reduction of processing efficiency compared to wild-type
L465A
10fold reduction of processing efficiency compared to wild-type
L478A
11fold reduction of processing efficiency compared to wild-type
L491A
processing efficiency reduced 7fold compared to wild-type tRNase Z
L499A
processing efficiency similar to wild-type tRNase Z
L507A
processing efficiency reduced 6fold compared to wild-type tRNase Z
N445A
5fold reduction of processing efficiency compared to wild-type
N449A
80fold reduction of processing efficiency compared to wild-type
P444A
5fold reduction of processing efficiency compared to wild-type
Q474A
750fold reduction of processing efficiency compared to wild-type
Q492A
processing efficiency similar to wild-type tRNase Z
R448A
625fold reduction of processing efficiency compared to wild-type
R477A
2600fold reduction of processing efficiency compared to wild-type
S441A
9fold reduction of processing efficiency compared to wild-type
S497A
processing efficiency reduced 495fold compared to wild-type tRNase Z
T439A
2.5fold reduction of processing efficiency compared to wild-type
T447A
2fold reduction of processing efficiency compared to wild-type
T471A
5fold reduction of processing efficiency compared to wild-type
T632A
HEAT-domain-variant
V450A
4fold reduction of processing efficiency compared to wild-type
V463A
6fold reduction of processing efficiency compared to wild-type
V476A
6fold reduction of processing efficiency compared to wild-type
V496A
processing efficiency similar to wild-type tRNase Z
Y472A
4fold reduction of processing efficiency compared to wild-type
Y479A
7fold reduction of processing efficiency compared to wild-type
Y495A
processing efficiency similar to wild-type tRNase Z
D212A
-
Asp(II) active site residue
D68A
-
Asp(I), active site residue
H141A
-
His(IV), active site residue
H248A
-
His(V), active site residue
H270A
-
His(VI), active site residue
H64A
-
His(I), active site residue
H66A
-
His(II), active site residue
H69A
-
His(III), active site residue
Q44S/Q46T
-
double mutant, cleavage of human pre-tRNA(Arg) after U75, very inefficiently
1641insG
-
frameshift mutation of ELAC2, lacks the C-terminal half, cannot increase suppression of ade6-704 in strain yYH1
D515A
-
tested for activity in presence of Mg2+ or Mn2+
D550A
-
Asp(I), active site residue
D666A
-
Asp(II), active site residue
E518A
-
tested for activity in presence of Mg2+ or Mn2+
E89A
-
influence on activity tested
F109S
-
influence on activity tested
G120Y
-
influence on activity tested
G281Y
-
influence on activity tested
G554L
-
tested for activity in presence of Mg2+ or Mn2+
H548A
-
His(II), active site residue
H551A
-
His(III), active site residue
H685A
-
tested for activity in presence of Mg2+ or Mn2+
H702A
-
His(V), active site residue
H724A
-
His(VI), active site residue
K282A
-
influence on activity tested
L539A
-
tested for activity in presence of Mg2+ or Mn2+
P493A
-
tested for activity in presence of Mg2+ or Mn2+
R497A
-
tested for activity in presence of Mg2+ or Mn2+
R718H
-
seems to be associated with the occurrence of prostate cancer
R781H
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
T520Q
-
tested for activity in presence of Mg2+ or Mn2+
D476A
overexpression of Trz2 in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
D578A
overexpression in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
H574A
overexpression in yYH1 cells does not result in an increase in nonsense suppression by tRNASer(UGA)-M1
I572K
inactivates the protein
Y571L
mutation does not result in a temperature-sensitive phenotype
Q45S/Q47T
-
very low activity
D190A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
D25A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
D52A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
F11P
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H134A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H222A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H244A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H48A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H50A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
H53A
-
in vitro 3'-processing in the presence of 10mM Mg2+ or 0.2 mM Mn2+
K162L
-
residue at the flexible arm of tRNase Z
K162L/R166L/K169L
-
residues at the flexible arm of tRNase Z
K162R
-
residue at the flexible arm of tRNase Z
K169L
-
residue at the flexible arm of tRNase Z
K169R
-
residue at the flexible arm of tRNase Z
R166L
-
residue at the flexible arm of tRNase Z
S31Q
-
cleavage site selection affected
S31Q/T33Q
-
cleavage site analyzed
T33Q
-
cleavage site selection affected
C25G
dimerization, RNA binding, 33% activity compared to wild-type
C25G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
C40G
dimerization, RNA binding, similar activity compared to wild-type
C40G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
E208A
dimerization, RNA binding, 55% activity compared to wild-type
E208A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
F51L
dimerization, RNA binding, similar activity compared to wild-type
F51L
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
G62V
dimerization, RNA binding, 26% activity compared to wild-type
G62V
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
P178A
dimerization, RNA binding, 74% activity compared to wild-type
P178A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
P64A
dimerization, RNA binding, similar activity compared to wild-type
P64A
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
R252G
dimerization, RNA binding, 26% activity compared to wild-type
R252G
-
variants of AthTRZ1 wild-type enzyme generated by mutagenesis
H65A
the mutation was introduced at the central histidine to slow down hydrolysis of precursor tRNA during cocrystallization
H65A
-
His(II), active site residue
K207A
increases in Km as compared to wild-type tRNase Z
K207A
significant reductions in kcat as compared to wild-type tRNase Z
A541T
-
seems to be associated with the occurrence of prostate cancer
A541T
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
H546A
-
His(I), active site residue
H546A
-
ELAC2 mutation, cannot increase suppression of ade6-704 in strain yYH1
S217L
-
seems to be associated with the occurrence of prostate cancer
S217L
-
overexpression of this missense mutant of ELAC2 can increase suppression of ade6-704 in strain yYH1
additional information
-
variants of tRNase Z enzymes generated by mutagenesis and properties of variants reviewed
additional information
Ala-scanning mutagenesis through five conserved loops on the carboxy side of motif II (motifs III, IV, HEAT,HST, and motif V) performed, pre-tRNA processing kinetics of the expressed variants studied
additional information
a conserved leucine at the ascending stalk/hand boundary causes practically the same increase in Km as the hand deletion, thus nearly eliminating its ability to bind substrate. Km also increases with substitutions in theGP(alpha4-alpha5) loop and at other conserved residues in the flexible arm hand predicted to contact substrate. Substitutions that reduce kcat are clustered in the beta10-beta11 loop