Exchangeability of the flagellin (FliC) and the cap protein (FliD) among different species in flagellar assembly1. Issue 1 (23rd October 2012)
- Record Type:
- Journal Article
- Title:
- Exchangeability of the flagellin (FliC) and the cap protein (FliD) among different species in flagellar assembly1. Issue 1 (23rd October 2012)
- Main Title:
- Exchangeability of the flagellin (FliC) and the cap protein (FliD) among different species in flagellar assembly1
- Authors:
- Inaba, Satoshi
Hashimoto, Manami
Jyot, Jeevan
Aizawa, Shin‐Ichi - Abstract:
- <abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Flagellar filament self‐assembles from the component protein, flagellin or FliC, with the aid of the capping protein, HAP2 or FliD. Depending on the helical parameters of filaments, flagella from various species are divided into three groups, family I, II, and III. Each family coincides with the traditional classification of flagella, peritrichous flagella, polar flagella, and lateral flagella, respectively. To elucidate the physico‐chemical properties of flagellin to separate families, we chose family I flagella and family II flagella and examined how well the exchangeability of a combination of FliC and/or FliD from different families is kept in filament formation. FliC or FliD of <italic>Salmonella enterica</italic> serovar Typhimurium (<italic>Salty</italic>; family I) were exchanged with those of <italic>Escherichia coli</italic> (<italic>Escco</italic>; family I) or <italic>Pseudomonas aeruginosa</italic> (<italic>Pseae</italic>; family II). In a <italic>Salty</italic> fliC deletion mutant, <italic>Escco</italic> FliC formed short filaments, but <italic>Pseae</italic> FliC did not form filaments. In a <italic>Salty</italic> fliD deletion mutant, both <italic>Escco</italic> FliD and <italic>Pseae</italic> FliD allowed <italic>Salty</italic> FliC to polymerize into short filaments. In conclusion, FliC can be exchanged among the same family but not between different families, while FliD serves as the<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Flagellar filament self‐assembles from the component protein, flagellin or FliC, with the aid of the capping protein, HAP2 or FliD. Depending on the helical parameters of filaments, flagella from various species are divided into three groups, family I, II, and III. Each family coincides with the traditional classification of flagella, peritrichous flagella, polar flagella, and lateral flagella, respectively. To elucidate the physico‐chemical properties of flagellin to separate families, we chose family I flagella and family II flagella and examined how well the exchangeability of a combination of FliC and/or FliD from different families is kept in filament formation. FliC or FliD of <italic>Salmonella enterica</italic> serovar Typhimurium (<italic>Salty</italic>; family I) were exchanged with those of <italic>Escherichia coli</italic> (<italic>Escco</italic>; family I) or <italic>Pseudomonas aeruginosa</italic> (<italic>Pseae</italic>; family II). In a <italic>Salty</italic> fliC deletion mutant, <italic>Escco</italic> FliC formed short filaments, but <italic>Pseae</italic> FliC did not form filaments. In a <italic>Salty</italic> fliD deletion mutant, both <italic>Escco</italic> FliD and <italic>Pseae</italic> FliD allowed <italic>Salty</italic> FliC to polymerize into short filaments. In conclusion, FliC can be exchanged among the same family but not between different families, while FliD serves as the cap protein even in different families, confirming that FliC is essential for determining families, but FliD plays a subsidiary role in filament formation. © 2012 Wiley Periodicals, Inc.</p> </abstract> … (more)
- Is Part Of:
- Biopolymers. Volume 99:Issue 1(2012)
- Journal:
- Biopolymers
- Issue:
- Volume 99:Issue 1(2012)
- Issue Display:
- Volume 99, Issue 1 (2012)
- Year:
- 2012
- Volume:
- 99
- Issue:
- 1
- Issue Sort Value:
- 2012-0099-0001-0000
- Page Start:
- 63
- Page End:
- 72
- Publication Date:
- 2012-10-23
- Subjects:
- Biopolymers -- Periodicals
Peptides -- Periodicals
Spectrum analysis -- Periodicals
572.33 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0282 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/bip.22141 ↗
- Languages:
- English
- ISSNs:
- 0006-3525
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.470000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3464.xml