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Literature summary for 3.1.26.12 extracted from

  • Beloglazova, N.; Brown, G.; Zimmerman, M.D.; Proudfoot, M.; Makarova, K.S.; Kudritska, M.; Kochinyan, S.; Wang, S.; Chruszcz, M.; Minor, W.; Koonin, E.V.; Edwards, A.M.; Savchenko, A.; Yakunin, A.F.
    A novel family of sequence-specific endoribonucleases associated with the clustered regularly interspaced short palindromic repeats (2008), J. Biol. Chem., 283, 20361-20371.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.26.12

Cloned(Commentary)

Cloned (Comment) Organism
expressed as a fusion with an N-terminal His6 tag in Escherichia coli strain BL21 (DE3) Saccharolobus solfataricus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method. The crystal structure of SSO1404 is solved at 1.6 A resolution revealing the first ribonuclease with a ferredoxin-like fold Saccharolobus solfataricus

Protein Variants

Protein Variants Comment Organism
D10A inactive mutant enzyme Saccharolobus solfataricus
D13A mutant enzyme shows wild-type level activity Saccharolobus solfataricus
D14A mutant enzyme shows wild-type level activity Saccharolobus solfataricus
D65A 2fold drop in activity compared to wild-type Saccharolobus solfataricus
F37A inactive mutant enzyme Saccharolobus solfataricus
N18A mutant enzyme shows wild-type level activity Saccharolobus solfataricus
Q33A slightly reduced activity Saccharolobus solfataricus
R17A very low activity Saccharolobus solfataricus
R19A very low activity Saccharolobus solfataricus
R31A inactive mutant enzyme Saccharolobus solfataricus
R67A mutant enzyme shows wild-type level activity Saccharolobus solfataricus
S35A slightly reduced activity Saccharolobus solfataricus
T12A 2fold drop in activity compared to wild-type Saccharolobus solfataricus
Y34A slightly reduced activity Saccharolobus solfataricus
Y9A very low activity Saccharolobus solfataricus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ 100 mM, required Saccharolobus solfataricus
Mg2+ 5 mM, required Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
11936
-
 2 * 11936, calculated from sequence Saccharolobus solfataricus
23700
-
 gel filtration Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97YC2
-
-
Saccharolobus solfataricus P2 Q97YC2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Saccharolobus solfataricus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
single-stranded RNA + H2O preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested Saccharolobus solfataricus ?
-
 ?
single-stranded RNA + H2O preferentially cleaves single-stranded RNAs within U-rich regions. Most cleavage sites contained one or two U. It cleaves the phosphodiester linkage on the 3'-side and generates 5'-phosphate- and 3'-hydroxyl-terminated oligonucleotides. The enzyme cleaves these substrates only in close proximity to the 5'- or 3'-ends suggesting that it requires the presence of a free RNA end. Oligoribonucleotides as short as 10 nt can serve as SSO1404 substrates. Tyr-9, Asp-10, Arg-17, Arg-19, Arg-31, and Phe-37 are important for enzymatic activity. Asp-10 might be the principal catalytic residue. No cleavage of dsRNA substrates prepared by annealing ssRNA substrates. No nuclease activity against either of the DNA substrates. The 39 nucleotide ssRNA substrate AAAUACG-/-U-/-U-/-UUCUCCAUUGUCAUAUUGCGCAUAAGUUGA shows the highest activity among the ssRNA substrates tested Saccharolobus solfataricus P2 ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 11936, calculated from sequence Saccharolobus solfataricus

Synonyms

Synonyms Comment Organism
SSO1404 locus name Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9
-
 Saccharolobus solfataricus

pH Range

pH Minimum pH Maximum Comment Organism
7 10
-
 Saccharolobus solfataricus

General Information

General Information Comment Organism
physiological function the role in the CRISPR-mediated anti-phage defense might involve degradation of phage or cellular mRNAs Saccharolobus solfataricus