RNase Y, 5 end sensitive endoribonuclease, involved in the degradation/ processing of mRNA
function
RNA processing and degradation
Genomic Context
categories
[category|SW 3|Information processing] → [category|SW 3.2|RNA synthesis and degradation] → [category|SW 3.2.4|RNases] → [category|SW 3.2.4.2|Endoribonucleases][category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation][category|SW 4|Lifestyles] → [category|SW 4.1|Exponential and early post-exponential lifestyles] → [category|SW 4.1.2|Biofilm formation] → [category|SW 4.1.2.5|Other proteins required for biofilm formation][category|SW 6|Groups of genes] → [category|SW 6.13|Quasi-essential genes][category|SW 6|Groups of genes] → [category|SW 6.2|Membrane proteins][SW|Categories] containing this gene/protein
[SW|RNAses], [SW|biofilm formation], [SW|membrane proteins]Gene
Coordinates on the chromosome (coding sequence)
1,767,310 -> 1,768,872
Phenotypes of a mutant
transcription profile resulting from ''[protein|search|rny]'' depletion: [http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE30430 GEO] [Pubmed|21815947]defect in spore [SW|germination] [Pubmed|22209493]the mutant is strongly impaired in [SW|sporulation], [SW|genetic competence] and many other phenotypes [Pubmed|23504012]it is not possible to construct a ''[SW|rnjA] [SW|rny]'' double mutant [Pubmed|23504012]The protein
Catalyzed reaction/ biological activity
[SW|RNase] Y cleaves [protein|search|S-box] [SW|riboswitch] RNAs ''in vivo'' and ''in vitro'' [Pubmed|19779461]preference for 5' monophosphorylated substrate ''in vitro'' [Pubmed|19779461]endonucleolytic cleavage [Pubmed|19779461]required for the processing of the ''[protein|search|gapA]'' operon mRNA [Pubmed|19193632]cleavage activity appears sensitive to downstream secondary structure [Pubmed|19779461][SW|RNase] Y initiates the degradation of ''[protein|search|rpsO]'' mRNA [Pubmed|20418391][SW|RNase] Y is responsible for the degradation of [SW|23S rRNA], [SW|16S rRNA], and mRNAs in aging spores [Pubmed|22209493][SW|RNase] Y cleaves the leader of the ''[protein|search|cwlO]'' mRNA at a stem-loop structure [Pubmed|24163346]3' end maturation of [rnpB|search|RNase P RNA] and [scr|search|scRNA] [Pubmed|25402410]Protein family
Member of the HD superfamily of metal-dependent phosphohydrolases; 2',3' cyclic nucleotide phosphodiesterase family (according to Swiss-Prot)[SW|Domains]
transmembrane domain (aa 5–24) [Pubmed|21803996]coiled-coiled domain (may form a leucine zipper) (aa 30-150) [Pubmed|21803996]KH domain (aa 210–280) [Pubmed|21803996,18422648][SW|HD domain] (aa 330–430) [Pubmed|21803996,9868367]C-terminal domain (aa 430-520) [Pubmed|21803996][SW|Cofactors]
requires Mg 2, which can be replaced by Zn 2 or Mn 2 ions, [Pubmed|19779461]Effectors of protein activity
appears sensitive to downstream secondary structure, [Pubmed|19779461][SW|Localization]
cell membrane, single-pass membrane protein [Pubmed|18763711,17005971,19820159,27708634]forms foci at the site of septation [Pubmed|23060960][SW|Interactions]
[Rny|search|RNase Y] forms dimers [Pubmed|21803996]part of the [SW|RNA degradosome][Rny|search|RNase Y]-[protein|search|PfkA] [Pubmed|19193632,21803996][Rny|search|RNase Y]-[protein|search|Eno] [Pubmed|19193632,21803996], K(D) of the interaction: 100 nM [Pubmed|22198292][Rny|search|RNase Y]-[protein|search|PnpA] [Pubmed|19193632,21803996,26797123], K(D) of the interaction: 5 nM [Pubmed|22198292][Rny|search|RNase Y]-[protein|search|RnjA] [Pubmed|19193632,21803996][rny|search|RNase Y]-[protein|search|CshA] [Pubmed|20572937,21803996][protein|search|DynA]-[rny|search|RNase Y] [Pubmed|23060960][SW|GapA]-[SW|Rny] [Pubmed|27449348], about 2% of all [SW|GapA] molecules participate in this interaction [Pubmed|27449348]Additional information
required for the processing of the ''[protein|search|gapA]'' operon mRNAExpression and Regulation
Operon
''[protein|search|rny]-[protein|search|ymdB]'' [Pubmed|21856853]''[protein|search|rny]'' [Pubmed|21856853]Regulation
constitutiveAdditional information
the [SW|transcription] terminator between ''[SW|rny]'' and ''[SW|ymdB]'' is strong and [SW|NusA]-independent [http://www.nature.com/articles/nmicrobiol20157 Reference]Biological materials
Mutant
4043 (''rny'' under p-spac control, ''cat''), GP193 (''rny'' under p-xyl control, ''cat''), both available in [SW|Jörg Stülke]'s labSSB447 (rny under P-spac control, erm) available in [SW|Putzer] labGP2501 (''[protein|search|rny]''::''spc''), available in [SW|Jörg Stülke]'s labExpression vector
N-terminal Strep-tag, expression in ''E. coli'', in [SW|pGP172]: pGP441, available in [SW|Jörg Stülke]'s labN-terminal Strep-tag, for [SW|SPINE], expression in ''B. subtilis'', in [SW|pGP380]: pGP775, available in [SW|Jörg Stülke]'s labC-terminal Strep-tag, for [SW|SPINE], expression in ''B. subtilis'', in [SW|pGP382]: pGP1852, available in [SW|Jörg Stülke]'s labExpression of RNase Y missing the N-terminal transmembrane domain (25aa) as an intein fusion in E. coli (no tag left in the purified protein) available in the [SW|Putzer] labwild type ''rny'', expression in ''B. subtilis'', in [SW|pBQ200]: pGP1201, available in [SW|Jörg Stülke]'s labthere is also a series of domain constructs present in [SW|pBQ200], all available in [SW|Jörg Stülke]'s labchromosomal expression of Rny-Strep, ''spc'': GP1033, available in [SW|Jörg Stülke]'s lablacZ fusion
pGP459 (in [protein|search|pAC7]), available in [SW|Jörg Stülke]'s labGFP fusion
B. subtilis 3569 (amyE:: (p-xyl rny-gfpmut1-spc)), available in [SW|Errington] labpGP1368 for chromosomal expression of rny-YFP, available in [SW|Jörg Stülke]'s labtwo-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s labFLAG-tag construct
GP1030 (spc, based on [SW|pGP1331]), available in [SW|Jörg Stülke]'s labAntibody
available in [SW|van Dijl] and in [SW|Jörg Stülke]'s labLabs working on this gene/protein
[SW|Ciaran Condon], IBPC Paris, France [http://www.ibpc.fr/UPR9073/equipe_Ciaran/AccueilCCondonGB.htm Homepage][SW|Harald Putzer], IBPC Paris, France [http://www.ibpc.fr/UPR9073/putzer/recherches_harald.htm Homepage][SW|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]References
Reviews
21957024,22568516,24064983,9868367,18422648,25292357 Original publications
21862575,22198292,22209493,22412379,23060960,23326572,21908660,21856853,21815947,24163346,18763711,19193632,17005971,19779461,19820159,20418391,20525796,20572937,21803996,21843271,23504012,25402410,26434553,26473962,26802042,26797123,26819068,26940229,21803996,27708634,27449348 Publications on homologs from other organisms
17951247,20385762,15853881,26473962