Linked Life Data

11293415

Source:http://linkedlifedata.com/resource/pubmed/id/11293415

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2001-4-9
pubmed:abstractText
The rate of production of Clostridium pasteurianum rubredoxin overexpressed in Escherichia coli was examined by electrospray ionization-Fourier transform ion cyclotron resonance (ESI-FTICR) mass spectrometry. Previous work had shown that this heterologous expression resulted in isolation of both iron-containing (FeRd) and zinc-containing (ZnRd) rubredoxins. In the present work, minimally processed cell lysates of E. coli were analyzed in order to monitor the production of FeRd and ZnRd. The sensitivity of the measurement favored FeRd relative to ZnRd, and this differential sensitivity was quantitated using previously separated and purified rubredoxins. A time course study indicated that ZnRd and FeRd are produced simultaneously during overexpression, but at different rates. The ratio of the concentration of ZnRd to FeRd increased in a linear fashion during 3 h following induction of overexpression. Since only FeRds have been reported from native bacteria and archaea, the data suggest that either Zn2+ is sequestered from rubredoxins during native biosynthesis or that ZnRds may have escaped detection in the native microorganisms. ESI-FTICR mass spectrometry is shown to be a useful tool for monitoring metal insertion during protein biosynthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0949-8257
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Analysis of metal incorporation during overexpression of Clostridium pasteurianum rubredoxin by electrospray FTICR mass spectrometry.
pubmed:affiliation
Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens 30602, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.