Linked Life Data

20815821

Source:http://linkedlifedata.com/resource/pubmed/id/20815821

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2010-10-25
pubmed:abstractText
Phage holins are small, lethal membrane proteins of two general types: canonical holins, like ? S105, which oligomerizes and forms large membrane holes of unprecedented size; and pinholins, like S(21) 68 of lambdoid phage 21, which forms homo-heptameric channels, or pinholes, with a lumen of <2 nm. Pinholes depolarize the membrane, leading to activation of secreted endolysins and murein degradation. S(21) 68 has two transmembrane domains, TMD1 and TMD2. TMD2 alone lines the pinhole, making heterotypic interactions involving two surfaces, A and B. Mutational analysis on S(21) 68 suggested that S(21) 68 initially forms inactive dimer, with TMD1 inhibiting TMD2 both in cis and trans. When TMD1 exits the membrane to the periplasm, it liberates TMD2 to participate in the pathway to pinhole formation. In this study, further mutational analysis suggests a refined pinhole formation pathway, with the existence of at least two intermediate states. We propose that the pathway begins in the activated dimer state, with a homotypic TMD2 interface involving the A surface. Evidence is presented for a further oligomeric state involving a heterotypic A:B interaction. Moreover, the data suggest that a glycine-zipper motif present in the A interface of TMD2 is involved in every stage downstream of the inactive dimer.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1365-2958
pubmed:author
pubmed:copyrightInfo
© 2010 Blackwell Publishing Ltd.
pubmed:issnType
Electronic
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
710-9
pubmed:dateRevised
2011-11-1
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Mapping the pinhole formation pathway of S21.
pubmed:affiliation
Department of Biochemistry and Biophysics, 2128 TAMU, Texas A&M University, College Station, TX 77843-2128, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural