File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Proteolytic processing of phage lambda tail protein gpH: timing of the cleavage

TitleProteolytic processing of phage lambda tail protein gpH: timing of the cleavage
Authors
Issue Date1983
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
Citation
Virology, 1983, v. 125 n. 2, p. 257-264 How to Cite?
AbstractWe describe a method for the rapid partial purification of intermediate structures of phage lambda tail assembly, using formaldehyde-fixed Escherichia coli cells to precipitate tail-related structures. The purification depends on the specific interaction between the E. coli lambda receptor protein and lambda tail protein gpJ. Protein compositions of tail assembly intermediates were analyzed to determine when in the assembly sequence the minor tail protein gpH is cleaved. gpH joins the tail precursor structure early in the pathway, during assembly of the initiator (a structure that becomes the tail tip). However, gpH is not cleaved until after initiator assembly is complete and after the tail shaft has polymerized onto the initiator. These results suggest that each gpH molecule is extended along the length of the tail. Our results also appear to eliminate an ambiguity in the tail assembly pathway determined by earlier experiments: we argue that gene G acts between genes H and M.
Persistent Identifierhttp://hdl.handle.net/10722/44205
ISSN
2015 Impact Factor: 3.2
2015 SCImago Journal Rankings: 1.805
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorTsui, L-Cen_HK
dc.contributor.authorHendrix, RWen_HK
dc.date.accessioned2007-09-12T03:48:58Z-
dc.date.available2007-09-12T03:48:58Z-
dc.date.issued1983en_HK
dc.identifier.citationVirology, 1983, v. 125 n. 2, p. 257-264en_HK
dc.identifier.issn0042-6822en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44205-
dc.description.abstractWe describe a method for the rapid partial purification of intermediate structures of phage lambda tail assembly, using formaldehyde-fixed Escherichia coli cells to precipitate tail-related structures. The purification depends on the specific interaction between the E. coli lambda receptor protein and lambda tail protein gpJ. Protein compositions of tail assembly intermediates were analyzed to determine when in the assembly sequence the minor tail protein gpH is cleaved. gpH joins the tail precursor structure early in the pathway, during assembly of the initiator (a structure that becomes the tail tip). However, gpH is not cleaved until after initiator assembly is complete and after the tail shaft has polymerized onto the initiator. These results suggest that each gpH molecule is extended along the length of the tail. Our results also appear to eliminate an ambiguity in the tail assembly pathway determined by earlier experiments: we argue that gene G acts between genes H and M.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviroen_HK
dc.relation.ispartofVirology-
dc.subject.meshBacteriophage lambda - analysisen_HK
dc.subject.meshEscherichia colien_HK
dc.subject.meshReceptors, virus - metabolismen_HK
dc.subject.meshViral proteins - metabolismen_HK
dc.subject.meshViral tail proteinsen_HK
dc.titleProteolytic processing of phage lambda tail protein gpH: timing of the cleavageen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0042-6822&volume=125&issue=2&spage=257&epage=264&date=1983&atitle=Proteolytic+processing+of+phage+lambda+tail+protein+gpH:+Timing+of+the+cleavageen_HK
dc.description.naturelink_to_subscribed_fulltexten_HK
dc.identifier.doi10.1016/0042-6822(83)90199-X-
dc.identifier.pmid6220513-
dc.identifier.isiWOS:A1983QJ42000001-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats