Rny

• Description: RNase Y, endoribonuclease, required for the processing of the gapA operon mRNA
  
  

Gene name	rny
Synonyms	ymdA
Essential	yes
Product	RNase Y
Function	required for the processing of the gapA operon mRNA
MW, pI	58,7 kDa, 5.39
Gene length, protein length	1560 bp, 520 amino acids
Immediate neighbours	pbpX, ymdB
Gene sequence (+200bp) corrected	Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context

The gene

Basic information

• Coordinates: 1766580 - 1768139

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry:

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: required for the processing of the gapA operon mRNA PubMed

• Protein family: 2',3' cyclic nucleotide phosphodiesterase family

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:
  • transmembrane domain (4–24)
  • KH domain (210–273)
  • HD domain (336–429)

• Modification:

• Cofactor(s): metal-dependent

• Effectors of protein activity:

• Interactions: Rny-PfkA, Rny-Eno, Rny-PnpA, Rny-RnjA PubMed

• Localization: Single-pass membrane protein PubMed

Database entries

• Structure:

• Swiss prot entry: [2]

• KEGG entry: [3]

• E.C. number: [4]

Additional information

required for the processing of the gapA operon mRNA

Expression and regulation

• Operon: rny-ymdB

• Sigma factor:

• Regulation: constitutive

• Regulatory mechanism:

• Additional information: there is a terminator between rny and ymdB, most transcripts terminate there

Biological materials

• Mutant: essential!!!!, 4043 (rny under p-spac control), GP193 (rny under p-xyl control), available in Stülke lab

• Expression vector:

N-terminal Strep-tag, expression in E. coli, in pGP172: pGP441, available in Stülke lab

N-terminal Strep-tag, for SPINE, expression in B. subtilis, in pGP380: pGP775 , available in Stülke lab

wild type rny, expression in B. subtilis, in pBQ200: pGP1201, available in Stülke lab

there is also a series of domain constructs present in pBQ200, all available in Stülke lab

• lacZ fusion: pGP459 (in pAC7), available in Stülke lab

• GFP fusion: B. subtilis 3569 (amyE:: (p-xyl rny-gfpmut1-spc)), available in Errington lab

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab

• Antibody: available in van Dijl and Stülke labs

Labs working on this gene/protein

Harald Putzer, IBPC Paris, France Homepage

Jörg Stülke, University of Göttingen, Germany Homepage

References

1. Commichau, F. M., Rothe, F. M., Herzberg, C., Wagner, E., Hellwig, D., Lehnik-Habrink, M., Hammer, E., Völker, U. & Stülke, J. (2009) Novel activities of glycolytic enzymes in Bacillus subtilis: Interactions with essential proteins involved in mRNA processing. Mol. Cell. Proteomics in press PubMed
2. Hunt, A., Rawlins, J. P., Thomaides, H. B., and Errington, J. (2006) Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 152, 2895-2907. PubMed