Difference between revisions of "Cca"
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Revision as of 13:44, 16 May 2013
- Description: tRNA nucleotidyltransferase, maturation of the single-copy tRNACys, which lacks an encoded CCA 3' end
| Gene name | cca |
| Synonyms | papS, ypjI |
| Essential | yes PubMed |
| Product | tRNA nucleotidyltransferase |
| Function | tRNA modification |
| Gene expression levels in SubtiExpress: cca | |
| MW, pI | 45 kDa, 8.041 |
| Gene length, protein length | 1191 bp, 397 aa |
| Immediate neighbours | birA, bshA |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU22450
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + tRNA(n) = diphosphate + tRNA(n+1) (according to Swiss-Prot)
- Protein family: the protein is similar to the E. coli poly(A) polymerase
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- Structure: 1MIV (Geobacillus stearothermophilus 44% identity)
- UniProt: P42977
- KEGG entry: [2]
- E.C. number: 2.7.7.25
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Heike Betat, Christiane Rammelt, Mario Mörl
tRNA nucleotidyltransferases: ancient catalysts with an unusual mechanism of polymerization.
Cell Mol Life Sci: 2010, 67(9);1447-63
[PubMed:20155482]
[WorldCat.org]
[DOI]
(I p)
Stefan Vörtler, Mario Mörl
tRNA-nucleotidyltransferases: highly unusual RNA polymerases with vital functions.
FEBS Lett: 2010, 584(2);297-302
[PubMed:19883645]
[WorldCat.org]
[DOI]
(I p)
Anne Neuenfeldt, Andrea Just, Heike Betat, Mario Mörl
Evolution of tRNA nucleotidyltransferases: a small deletion generated CC-adding enzymes.
Proc Natl Acad Sci U S A: 2008, 105(23);7953-8
[PubMed:18523015]
[WorldCat.org]
[DOI]
(I p)
Yong Xiong, Thomas A Steitz
A story with a good ending: tRNA 3'-end maturation by CCA-adding enzymes.
Curr Opin Struct Biol: 2006, 16(1);12-7
[PubMed:16364630]
[WorldCat.org]
[DOI]
(P p)
Original publications
Juan Campos-Guillén, Jackeline Lizzeta Arvizu-Gómez, George H Jones, Gabriela Olmedo-Alvarez
Characterization of tRNA(Cys) processing in a conditional Bacillus subtilis CCase mutant reveals the participation of RNase R in its quality control.
Microbiology (Reading): 2010, 156(Pt 7);2102-2111
[PubMed:20360175]
[WorldCat.org]
[DOI]
(I p)
Hyundae D Cho, Christophe L M J Verlinde, Alan M Weiner
Reengineering CCA-adding enzymes to function as (U,G)- or dCdCdA-adding enzymes or poly(C,A) and poly(U,G) polymerases.
Proc Natl Acad Sci U S A: 2007, 104(1);54-9
[PubMed:17179213]
[WorldCat.org]
[DOI]
(P p)
Patricia Bralley, Samantha A Chang, George H Jones
A phylogeny of bacterial RNA nucleotidyltransferases: Bacillus halodurans contains two tRNA nucleotidyltransferases.
J Bacteriol: 2005, 187(17);5927-36
[PubMed:16109934]
[WorldCat.org]
[DOI]
(P p)
Fang Li, Yong Xiong, Jimin Wang, HyunDae D Cho, Kozo Tomita, Alan M Weiner, Thomas A Steitz
Crystal structures of the Bacillus stearothermophilus CCA-adding enzyme and its complexes with ATP or CTP.
Cell: 2002, 111(6);815-24
[PubMed:12526808]
[WorldCat.org]
[DOI]
(P p)
L C Raynal, H M Krisch, A J Carpousis
The Bacillus subtilis nucleotidyltransferase is a tRNA CCA-adding enzyme.
J Bacteriol: 1998, 180(23);6276-82
[PubMed:9829937]
[WorldCat.org]
[DOI]
(P p)
Operon and expression
Ahmed Gaballa, Gerald L Newton, Haike Antelmann, Derek Parsonage, Heather Upton, Mamta Rawat, Al Claiborne, Robert C Fahey, John D Helmann
Biosynthesis and functions of bacillithiol, a major low-molecular-weight thiol in Bacilli.
Proc Natl Acad Sci U S A: 2010, 107(14);6482-6
[PubMed:20308541]
[WorldCat.org]
[DOI]
(I p)
