Functional chimeras of flagellar stator proteins between E. coli MotB and Vibrio PomB at the periplasmic region in Vibrio or E. coli. Issue 2 (29th January 2015)
- Record Type:
- Journal Article
- Title:
- Functional chimeras of flagellar stator proteins between E. coli MotB and Vibrio PomB at the periplasmic region in Vibrio or E. coli. Issue 2 (29th January 2015)
- Main Title:
- Functional chimeras of flagellar stator proteins between E. coli MotB and Vibrio PomB at the periplasmic region in Vibrio or E. coli
- Authors:
- Nishino, Yuuki
Onoue, Yasuhiro
Kojima, Seiji
Homma, Michio - Abstract:
- <abstract abstract-type="main" id="mbo3240-abs-0001"> <title>Abstract</title> <p>The bacterial flagellar motor has a stator and a rotor. The stator is composed of two membrane proteins, MotA and MotB in <italic>Escherichia coli</italic> and PomA and PomB in <italic>Vibrio alginolyticus</italic>. The <italic>Vibrio</italic> motor has a unique structure, the T ring, which is composed of MotX and MotY. Based on the structural information of PomB and MotB, we constructed three chimeric proteins between PomB and MotB, named PotB<sub>91</sub>, PotB<sub>129, </sub> and PotB<sub>138</sub>, with various chimeric junctions. When those chimeric proteins were produced with PomA in a Δ<italic>motAB</italic> strain of <italic>E. coli</italic> or in Δ<italic>pomAB</italic> and Δ<italic>pomAB</italic> Δ<italic>motX</italic> strains of <italic>Vibrio</italic>, all chimeras were functional in <italic>E. coli</italic> or <italic>Vibrio</italic>, either with or without the T ring, although the motilities were very weak in <italic>E. coli</italic>. Furthermore, we could isolate some suppressors in <italic>E. coli</italic> and identified the mutation sites on PomA or the chimeric B subunit. The weak function of chimeric PotBs in <italic>E. coli</italic> is derived mainly from the defect in the rotational switching of the flagellar motor. In addition, comparing the motilities of chimera strains in Δ<italic>pomAB</italic>, PotB<sub>138</sub> had the highest motility. The difference between the<abstract abstract-type="main" id="mbo3240-abs-0001"> <title>Abstract</title> <p>The bacterial flagellar motor has a stator and a rotor. The stator is composed of two membrane proteins, MotA and MotB in <italic>Escherichia coli</italic> and PomA and PomB in <italic>Vibrio alginolyticus</italic>. The <italic>Vibrio</italic> motor has a unique structure, the T ring, which is composed of MotX and MotY. Based on the structural information of PomB and MotB, we constructed three chimeric proteins between PomB and MotB, named PotB<sub>91</sub>, PotB<sub>129, </sub> and PotB<sub>138</sub>, with various chimeric junctions. When those chimeric proteins were produced with PomA in a Δ<italic>motAB</italic> strain of <italic>E. coli</italic> or in Δ<italic>pomAB</italic> and Δ<italic>pomAB</italic> Δ<italic>motX</italic> strains of <italic>Vibrio</italic>, all chimeras were functional in <italic>E. coli</italic> or <italic>Vibrio</italic>, either with or without the T ring, although the motilities were very weak in <italic>E. coli</italic>. Furthermore, we could isolate some suppressors in <italic>E. coli</italic> and identified the mutation sites on PomA or the chimeric B subunit. The weak function of chimeric PotBs in <italic>E. coli</italic> is derived mainly from the defect in the rotational switching of the flagellar motor. In addition, comparing the motilities of chimera strains in Δ<italic>pomAB</italic>, PotB<sub>138</sub> had the highest motility. The difference between the origin of the <italic>α</italic>1 and <italic>α</italic>2 helices, <italic>E. coli</italic> MotB or <italic>Vibro</italic> PomB, seems to be important for motility in <italic>E. coli</italic> and especially in <italic>Vibrio</italic>.</p> </abstract> … (more)
- Is Part Of:
- MicrobiologyOpen. Volume 4:Issue 2(2015:Apr.)
- Journal:
- MicrobiologyOpen
- Issue:
- Volume 4:Issue 2(2015:Apr.)
- Issue Display:
- Volume 4, Issue 2 (2015)
- Year:
- 2015
- Volume:
- 4
- Issue:
- 2
- Issue Sort Value:
- 2015-0004-0002-0000
- Page Start:
- 323
- Page End:
- 331
- Publication Date:
- 2015-01-29
- Subjects:
- Microbiology -- Periodicals
579 - Journal URLs:
- http://onlinelibrary.wiley.com/ ↗
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2045-8827 ↗ - DOI:
- 10.1002/mbo3.240 ↗
- Languages:
- English
- ISSNs:
- 2045-8827
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 3070.xml