Wed Jan 25 2017 10:16:53 GMT+0100 (CET)2025-05-25 08:48:21
description
RNase J1
RNase J1, important for the degradation of RNA fragments containing transcription terminators, resolves stalled transcription complexes
locus
BSU14530
BSU_14530
ec
outlinks
bsu
BSU14530
BSU_14530
[SW|Categories] containing this gene/protein
[SW|RNAses], [SW|essential genes]
Gene
Coordinates on the chromosome (coding sequence)
1,523,118 -> 1,524,785
Gene
Phenotypes of a mutant
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]
growth is strongly impaired (doubling time in complex medium 145 minutes vs. 43 minutes for the wild type) [pubmed|26883633]
the mutant is strongly impaired in [SW|sporulation], [SW|genetic competence] and many other phenotypes [Pubmed|23504012]
it is not possible to construct a ''[[gene|rnjA]] [[gene|rny]]'' double mutant [Pubmed|23504012]
The protein
Catalyzed reaction/ biological activity
endonuclease and 5'-3' exonuclease
degrades [SW|SR5] and ''[SW|gapA]'' RNAs [SW|27449348]
endonuclease and 5'-3' exonuclease
degrades [[protein|SR5]] and ''[[gene|gapA]]'' RNAs [pubmed|27449348]
degrades [[gene|yflS ]]mRNA [pubmed|28436820]
resolves stalled transcription complexes by a “torpedo” mechanism, whereby RNase J1 degrades the nascent RNA and causes the transcription complex to disassemble upon collision with [SW|RNA polymerase] [pubmed|31840842]
The protein
Protein family
RNase J subfamily (according to Swiss-Prot)
[SW|metallo-beta-lactamase superfamily] (according to UniProt)
The protein
Paralogous protein(s)
[[protein|RnjB]]
[[this]]
The protein
Effectors of protein activity
initeraction with [SW|GapA]-[SW|YkzW] stimulates activity [Pubmed|27449348]
initeraction with [[protein|GapA]]-[[protein|Sr1]] stimulates activity [Pubmed|27449348]
a NAD-cap stabilizes RNA against exonucleolytic attack by RNase J1 [pubmed|30110644]
The protein
[SW|Interactions]
part of the [SW|RNA degradosome] [Pubmed|19193632]
[[protein|RnjA]]-[[protein|RnjB]] [Pubmed|19193632,20025672,27708634]
[[protein|RnjA]]-[[protein|PfkA]] [Pubmed|19193632]
[[protein|RnjA]]-[[protein|PnpA]] [Pubmed|19193632], K(D) of the interaction: 250 nM [Pubmed|22198292]
[[protein|RnjA]]-[[protein|Rny]] [Pubmed|19193632,21803996]
[[protein|RnjA]]-[[protein|CshA]] [Pubmed|20572937]
[SW|GapA]-[SW|RnjA] [Pubmed|27449348], about 1% of all [SW|GapA] molecules participate in this interaction [Pubmed|27449348], this interaction is stabilized in the presence of [SW|YkzW] [Pubmed|27449348]
The protein
Additional information
subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]
required for ''[[protein|thrS]]'' RNA processing, involved in maturation of the 5’-end of the16S rRNA
subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]
required for [[gene|thrS]] RNA processing, involved in maturation of the 5-end of the 16S rRNA
Expression and Regulation
Operon
''[[protein|rpoY]]-[[protein|rnjA]]'' [Pubmed|24187087]
Expression and Regulation
[SW|Sigma factor]
[[protein|SigA]] [Pubmed|24187087]
Expression and Regulation
Additional information
subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]
translation of [[protein|YkzG]] and [[protein|RnjA]] is coupled, and this coupling is required for efficient expression of [[rnjA|RNase J1]] [PubMed|24187087]
Biological materials
Mutant
GP41 (''rnjA'' under control of p(xyl)), available in [SW|Jörg Stülke]'s lab
SSB342 (''rnjA'' under pspac), cat, available in [SW|Harald Putzer] lab
GP2506 (''[[protein|rnjA]]''::''spc''), available in [SW|Jörg Stülke]'s lab
GP41 (''rnjA'' under control of p(xyl)), available in [SW|Jörg Stülke]'s lab
SSB342 (''rnjA'' under pspac), cat, available in [SW|Harald Putzer]'s lab
GP2506 ([[gene|rnjA]]::''spc''), available in [SW|Jörg Stülke]'s lab
Biological materials
Expression vector
for chromosomal expression of RNase J1-Strep (spc): GP1034, available in [SW|Jörg Stülke]'s lab
for chromosomal expression of RNase J1-Strep (cat): GP1042, available in [SW|Jörg Stülke]'s lab
Biological materials
lacZ fusion
pGP418 (in [[protein|pAC7]]), available in [SW|Jörg Stülke]'s lab
pGP418 (in [SW|pAC7]), available in [SW|Jörg Stülke]'s lab
Biological materials
two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s lab
B. pertussis adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s lab, [pubmed|19193632]
Labs working on this gene/protein
[SW|Harald Putzer], IBPC Paris, France [http://www.ibpc.fr/UPR9073/putzer/recherches_harald.htm Homepage]
[SW|David Bechhofer], Mount Sinai School, New York, USA [http://www.mountsinai.org/Research/Centers Laboratories and Programs/Bechhofer Laboratory?citype=Physician&ciid=Bechhofer David H 1255565 Homepage]
[SW|Ciaran Condon], IBPC, Paris, France [http://www.ibpc.fr/UPR9073/condon/index_en.html Homepage]
References
Reviews
References
Original publications
proteinLength
555
geneLength
1668
Gene
Coordinates
1,523,118 1,524,785
Expression and Regulation
Operons
[[this]]
Expression and Regulation
Other regulations
[[this]]
Biological materials
Expression vectors
for chromosomal expression of RNase J1-Strep (spc): GP1034, available in [SW|Jörg Stülke]'s lab
for chromosomal expression of RNase J1-Strep (cat): GP1042, available in [SW|Jörg Stülke]'s lab
pGP1441: IPTG inducible expression, purification in ''E. coli'' with N-terminal Strep-tag, in [SW|pGP172], available in [SW|Jörg Stülke]'s lab
Biological materials
GFP fusion
GP1694 (in pHJS-105 [Pubmed|26110430]), expression of '' rnjA-sfGFP''::''spc'' under a xylose-inducible promoter in '' B. subtilis'', available in [SW|Jörg Stülke]'s lab [Pubmed|27708634]
GP1722 (in [SW|pBP43]), expression of '' rnjA-GFP''::''spc'' under the native promoter, available in [SW|Jörg Stülke]'s lab [Pubmed|27708634]
labs
[SW|Harald Putzer], IBPC Paris, France [http://www.ibpc.fr/UPR9073/putzer/recherches_harald.htm Homepage]
[SW|David Bechhofer], Mount Sinai School, New York, USA [http://www.mountsinai.org/Research/Centers Laboratories and Programs/Bechhofer Laboratory?citype=Physician&ciid=Bechhofer David H 1255565 Homepage]
[SW|Ciaran Condon], IBPC, Paris, France [http://www.ibpc.fr/UPR9073/condon/index_en.html Homepage]