HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ohkawa, I. Articles by Webster, R. E. Search for Related Content PubMed PubMed Citation Articles by Ohkawa, I. Articles by Webster, R. E. Social Bookmarking                      What's this?

J. Biol. Chem., Vol. 256, Issue 19, 9951-9958, Oct, 1981

The orientation of the major coat protein of bacteriophage f1 in the cytoplasmic membrane of Escherichia coli

I Ohkawa and RE Webster

The orientation of the major coat (B) protein of the bacteriophage f1, an integral membrane protein in the cytoplasmic membrane of infected Escherichia coli, was examined. Pyridoxal 5'-phosphate and [3H]NaBH4 were used to label the cytoplasmic membrane proteins in spheroplasts and membrane vesicles of E. coli infected with bacteriophage f1. Under the conditions described, tritium incorporation was almost completely dependent on the presence of pyridoxal 5'-phosphate and little if any of the cytoplasmic proteins were labeled when the reaction was applied to intact spheroplasts. The major coat protein was isolated from the cytoplasmic membranes labeled in this manner and the chymotryptic peptides were analyzed for the presence of tritium in the pyridoxamine 5'-phosphate conjugate. When the proteins were labeled in the intact spheroplast, only the NH2-terminal chymotryptic peptide of the coat protein was labeled. If the proteins were labeled during osmotic lysis of the spheroplasts or in isolated vesicles, the chymotryptic peptide containing the COOH terminus of the coat protein as well as the NH2- terminal peptide was labeled. The NH2-terminal peptide was labeled to approximately the same extent as occurred in the intact spheroplast. These results are consistent with the hypothesis that the mature f1 coat protein asymmetrically spans the cytoplasmic membrane of the infected host with its NH2 terminus exposed on the outside and COOH terminus exposed on the cytoplasmic surface.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. M. Click and R. E. Webster The TolQRA Proteins Are Required for Membrane Insertion of the Major Capsid Protein of the Filamentous Phage f1 during Infection J. Bacteriol., April 1, 1998; 180(7): 1723 - 1728. [Abstract] [Full Text]

				R Nambudripad, W Stark, S. Opella, and L Makowski Membrane-mediated assembly of filamentous bacteriophage Pf1 coat protein Science, May 31, 1991; 252(5010): 1305 - 1308. [Abstract] [PDF]

				W. Wickner and H. Lodish Multiple mechanisms of protein insertion into and across membranes Science, October 25, 1985; 230(4724): 400 - 407. [Abstract] [PDF]