SubtiBank SubtiBank
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Sun Dec 18 2016 20:27:19 GMT+0100 (CET)2017-02-27 15:02:04

[SW|Categories] containing this gene/protein

[SW|RNAses], [SW|essential genes]

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]

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

endonuclease and 5'-3' exonuclease

degrades [[protein|SR5]] and ''[[gene|gapA]]'' RNAs [SW|27449348]

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 the16S 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] 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

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

References

Reviews

20458164, 21334965, 21893280, 23403287, 21957024, 22568516, 24064983, 25292357

20458164, 21334965, 21893280, 23403287, 21957024, 22568516, 24064983, 25292357, 27750368

proteinLength

555

geneLength

1665

The protein

Effectors of protein activity

initeraction with [[protein|GapA]]-[[protein|Sr1]] stimulates activity [Pubmed|27449348]

Expression and Regulation

[[this]]

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]