ISCID Forums


Post New Topic  Post A Reply
my profile | search | faq | forum home
  next oldest topic   next newest topic
» ISCID Forums   » General   » News & Features   » Rusty, jammed, and well-oiled hinges: (FliG mutations in flagellar rotor)

   
Author Topic: Rusty, jammed, and well-oiled hinges: (FliG mutations in flagellar rotor)
David L. Hagen
Member
Member # 323

Icon 1 posted 09. August 2006 14:37      Profile for David L. Hagen   Email David L. Hagen   Send New Private Message       Edit/Delete Post 
Rusty, jammed, and well-oiled hinges: Mutations affecting the interdomain region of FliG, a rotor element of the Escherichia coli flagellar motor.
* Van Way SM, * Millas SG, * Lee AH, * Manson MD. Department of Biology, Texas A&M University, College Station, Texas 77843, USA.

J Bacteriol. 2004 May;186(10):3173-81.

Abstract
The FliG protein is a central component of the bacterial flagellar motor. It is one of the first proteins added during assembly of the flagellar basal body, and there are 26 copies per motor. FliG interacts directly with the Mot protein complex of the stator to generate torque, and it is a crucial player in switching the direction of flagellar rotation from clockwise (CW) to counterclockwise and vice versa. A primarily helical linker joins the N-terminal assembly domain of FliG, which is firmly attached to the FliF protein of the MS ring of the basal body, to the motility domain that interacts with MotA/MotB. We report here the results of a mutagenic analysis focused on what has been called the hinge region of the linker. Residue substitutions in this region generate a diversity of phenotypes, including motors that are strongly CW biased, infrequent switchers, rapid switchers, and transiently or permanently paused. Isolation of these mutants was facilitated by a "sensitizing" mutation (E232G) outside of the hinge region that was accidentally introduced during cloning of the chromosomal fliG gene into our vector plasmid. This mutation partially interferes with flagellar assembly and accentuates the defects associated with mutations that by themselves have little phenotypic consequence. The effects of these mutations are analyzed in the context of a conformational-coupling model for motor switching and with respect to the structure of the C-terminal 70% of FliG from Thermotoga maritima.
PMID: 15126479 [PubMed - indexed for MEDLINE]

Full Article:
Rusty, Jammed, and Well-Oiled Hinges
Rusty, Jammed, and Well-Oiled Hinges
---------------
Note distinctions between
* full function,
* reduced function from mutations, and
* no function due to mutations.

IP: Logged


All times are East Coast  
Post New Topic  Post A Reply Close Topic    Move Topic    Delete Topic    Top Topic next oldest topic   next newest topic
 - Printer-friendly view of this topic
Hop To:

Contact Us | ISCID

All content © ISCID and content contributor 2001-2003

The ISCID Forums are aimed at generating insight into the nature of complex systems (e.g. biological complexity, organizational complexity, etc.) and the ontological status of purpose, especially from the vantage point of various information- and design-theoretic models.

Indexed by UBB Spider Hack  |  Powered by Infopop Corporation UBB.classicTM 6.3.1.1

PCID | Encyclopedia | Brainstorms | The Archive | News | Essay Contests | Chat Events | Membership