MUTATIONS IN BACILLUS SUBTILIS WHICH INFLUENCE THE ACTIVITY OF A PROMOTER RECOGNIZED BY A MINOR FORM OF RNA POLYMERASE (E-σB)

Author(s):  
A.K. Benson ◽  
A. Stevenson ◽  
W.G. Haldenwang
1985 ◽  
Vol 161 (2) ◽  
pp. 515-522 ◽  
Author(s):  
C L Truitt ◽  
G L Ray ◽  
J E Trempy ◽  
Z Da-Jian ◽  
W G Haldenwang

2002 ◽  
Vol 184 (2) ◽  
pp. 596-599 ◽  
Author(s):  
Madhulika Dixit ◽  
Charuta S. Murudkar ◽  
K. Krishnamurthy Rao

ABSTRACT Epr is a minor extracellular protease secreted by Bacillus subtilis 168. In this study, we show that epr is transcribed by EςD, the RNA polymerase associated with transcription of genes involved in chemotaxis and motility. Disruption of epr abolished swarming of Bacillus subtilis, suggesting its involvement in motility.


2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Hao-Hong Pei ◽  
Tarek Hilal ◽  
Zhuo A. Chen ◽  
Yong-Heng Huang ◽  
Yuan Gao ◽  
...  

AbstractCellular RNA polymerases (RNAPs) can become trapped on DNA or RNA, threatening genome stability and limiting free enzyme pools, but how RNAP recycling into active states is achieved remains elusive. In Bacillus subtilis, the RNAP δ subunit and NTPase HelD have been implicated in RNAP recycling. We structurally analyzed Bacillus subtilis RNAP-δ-HelD complexes. HelD has two long arms: a Gre cleavage factor-like coiled-coil inserts deep into the RNAP secondary channel, dismantling the active site and displacing RNA, while a unique helical protrusion inserts into the main channel, prying the β and β′ subunits apart and, aided by δ, dislodging DNA. RNAP is recycled when, after releasing trapped nucleic acids, HelD dissociates from the enzyme in an ATP-dependent manner. HelD abundance during slow growth and a dimeric (RNAP-δ-HelD)2 structure that resembles hibernating eukaryotic RNAP I suggest that HelD might also modulate active enzyme pools in response to cellular cues.


FEBS Letters ◽  
1971 ◽  
Vol 13 (5) ◽  
pp. 269-274 ◽  
Author(s):  
J.C.C. Maia ◽  
P. Kerjan ◽  
J. Szulmajster

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