Effect of site-directed replacement mutations to channel-lining arginine in flagellin on protein transport and motility in Salmonella typhimurium
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Authors
Love, Chloe R.
Issue Date
2019
Type
Presentation
Language
en_US
Keywords
Alternative Title
Abstract
The bacterial flagellum is a highly conserved, autoassembling
structure which enables motility. The
flagellum consists of three parts: a basal body inside the
cell, a hook structure, and an external flagellar filament,
which is typically several times longer than the cell body.
The flagellar filament is a narrow tube-like structure
composed of a single protein, flagellin, which is diffused
down the channel at the center of the filament as it is
assembled. Four amino acids constitute the flagellar
channel. The terminal amino acid which lines this channel
is arginine, which is polar and carries a positive charge.
This study endeavored to ascertain whether the positive
charge, polarity, or size of arginine is necessary for protein
transport and successful auto-assembly of the flagellar
filament.
Description
1 Broadside. 48"W x 36"H
Citation
Publisher
Kalamazoo, Mich. : Kalamazoo College
License
U.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.