Cca

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  • 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
Cca context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Cca expression.png
























Categories containing this gene/protein

translation, essential genes

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)
  • KEGG entry: [2]

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