Back to results

University of Illinois at Urbana-Champaign

Covalent post-translational modification of proteins in Escherichia coli: Genetic and biochemical studies of biotin and lipoic acid biosynthesis and function

Abstract

dc:description

I have identified four distinct classes of mutants involved in either lipoic acid biosynthesis or the covalent attachment of lipoic acid to proteins in E. coli. Two of these classes of mutants were isolated as Tn1000dKn insertion mutants and both classes map to min 14.5 on the E. coli chromosome. The other two classes of mutants were isolated as spontaneous selenolipoic acid resistant (slr) mutants. Selenolipoic acid was shown to be a potent inhibitor of wild type E. coli.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Microbiology
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2011

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Reed, Kelynne Elizabeth
Contributors dc:contributor
  • Cronan, John E.

Subjects

dc:subject × 1

Rights

dc:rights
Statement dc:rights
  • Copyright 1992 Reed, Kelynne Elizabeth
Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
AAI9305663
(UMI)AAI9305663
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/22104

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Reed, Kelynne Elizabeth. Covalent post-translational modification of proteins in Escherichia coli: Genetic and biochemical studies of biotin and lipoic acid biosynthesis and function. Dissertation thesis, University of Illinois at Urbana-Champaign, 2011. http://hdl.handle.net/2142/22104