Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-4-6
pubmed:abstractText
PS1 is a protein translocated across the cytoplasmic membrane of Corynebacterium glutamicum, a Gram-positive bacterium. Western blots of whole cell extracts showed the presence of two bands associated with the mature and the precursor forms. Addition of chloramphenicol led to the disappearance of the precursor form while dissipation of the protonmotive force (delta microH) prior to the addition of chloramphenicol prevented the maturation of the precursor. Dissipation of delta microH prior to a pulse chase experiment resulted in a complete block on translocation; regeneration of delta microH allowed the translocation of PS1 synthesized in its absence. On the other hand, dissipation of delta microH immediately after a pulse period had little effect on PS1 secretion. Lowering the temperature to 10 degrees C at the end of the pulse period completely inhibited secretion. The efficiency of secretion as a function of increasing temperature followed closely the order-to-disorder transition of the membrane lipids as detected by fluorescence anisotropy of diphenylhexatriene. Taken together, the results show that delta microH and the state of the lipids affect different steps of PS1 secretion.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
1146
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
97-105
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Role of the protonmotive force and of the state of the lipids in the in vivo protein secretion in Corynebacterium glutamicum, a gram-positive bacterium.
pubmed:affiliation
Laboratoire des Biomembranes, CNRS (UA 1116 and GDR 961), Université de Paris-Sud, Orsay, France.
pubmed:publicationType
Journal Article