Abstract:
:FpvR is a presumed cytoplasmic membrane-associated anti-sigma factor that controls the activities of extracytoplasmic function sigma factors PvdS and FpvI responsible for transcription of pyoverdine biosynthetic genes and the ferric pyoverdine receptor gene, fpvA, respectively. Using deletion analysis and an in vivo bacterial two-hybrid system, FpvR interaction with these sigma factors was confirmed and shown to involve the cytoplasmic N-terminal 67 amino acid resides of FpvR. FpvR bound specifically to a C-terminal region of FpvI corresponding to region 4 of the sigma(70) family of sigma factors. FpvR and FpvI mutant proteins compromised for this interaction were generated by random and site-directed PCR mutagenesis and invariably contained secondary structure-altering proline substitution in predicted alpha-helices within the FpvR N terminus or FpvI region 4. PvdS was shown to bind to the same N-terminal region of FpvR, and FpvR mutations compromising FpvI binding also compromised PvdS binding, although some mutations had a markedly greater impact on PvdS binding. Apparently, these two sigma factors bind to FpvR in a substantially similar but not identical fashion. Intriguingly, defects in FpvR binding correlated with a substantial drop in yields of the FpvI and to a lesser extent PvdS sigma factors, suggesting that FpvR-bound FpvI and PvdS are stable while free and active sigma factor is prone to turnover.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Rédly GA,Poole Kdoi
10.1128/JB.187.16.5648-5657.2005keywords:
subject
Has Abstractpub_date
2005-08-01 00:00:00pages
5648-57issue
16eissn
0021-9193issn
1098-5530pii
187/16/5648journal_volume
187pub_type
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更新日期:1971-09-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1989-03-01 00:00:00
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pub_type: 杂志文章
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更新日期:1989-07-01 00:00:00