Publication Date:
1987-12-04
Description:
The major coat protein of bacteriophage M13 is synthesized as a precursor, the procoat, with a typical leader (signal) sequence of 23 residues at its NH2-terminus. A fusion protein that contains the NH2-terminal 141 residues of cytoplasmic ribulokinase and all but the first ten residues of M13 procoat was made. The fusion protein inserts into the plasma membrane of Escherichia coli and is processed by leader peptidase to give rise to a leader peptide of 155 residues and the mature coat protein of 50 residues. The NH2-terminus of the leader peptide remains in the cytoplasm and is protected from protease added to the medium outside of the cell. This indicates that M13 procoat inserts into the membrane as a loop structure and that the NH2-terminus of a leader peptide remains within the cytoplasm during membrane insertion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuhn, A -- New York, N.Y. -- Science. 1987 Dec 4;238(4832):1413-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Microbiology Department, University of Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3317833" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Capsid/*metabolism
;
Coliphages/*metabolism
;
Escherichia coli/metabolism
;
Membrane Proteins/*metabolism
;
Molecular Sequence Data
;
Protein Conformation
;
Protein Precursors/metabolism
;
Protein Processing, Post-Translational
;
Protein Sorting Signals/metabolism
;
Recombinant Fusion Proteins/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
