Linked Life Data

16822698

Source:http://linkedlifedata.com/resource/pubmed/id/16822698

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2006-7-25
pubmed:abstractText
Over last two decades many researchers have demonstrated the mechanisms of how the Escherichia coli chaperonin GroEL and GroES work in the binding and folding of different aggregation prone substrate proteins both in vivo and in vitro. However, preliminary aspects, such as influence of co-expressing GroEL and GroES on the over expression of other recombinant proteins in E. coli cells and subsequent growth aspects, as well as the conditions for optimum production of recombinant proteins in presence of recombinant chaperones have not been properly investigated. In the present study we have demonstrated the temperature dependent growth characteristics of E. coli cells, which are over expressing recombinant aconitase and how the co-expression of E. coli chaperonin GroEL and GroES influence the growth rate of the cells and in vivo folding of recombinant aconitase. Presence of co-expressed GroEL reduces the aconitase over-expression drastically; however, exogenous GroEL & GroES together compensate this reduction. For the aconitase over-expressing cells the growth rate decreases by 30% at 25 degrees C when compared with the M15 E. coli cells, however, there is an increase of 20% at 37 degrees C indicating the participation of endogenous chaperonin in the folding of a fraction of over expressed aconitase. However, in presence of co-expressed GroEL and GroES the growth rate of aconitase producing cells was enhanced by 30% at 37 degrees C confirming the assistance of exogenous chaperone system for the folding of recombinant aconitase. Optimum in vivo folding of aconitase requires co-production of complete E. coli chaperonin machinery GroEL and GroES together.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1975-85
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Co-expression of chaperonin GroEL/GroES enhances in vivo folding of yeast mitochondrial aconitase and alters the growth characteristics of Escherichia coli.
pubmed:affiliation
Department of Biochemical Engineering and Biotechnology, Indian Institute of Technology, Delhi, Hauz Khas, New Delhi 110016, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't