Accessibility and Environment Probing Using Cysteine Residues Introduced along the Putative Transmembrane Domain of the Major Coat Protein of Bacteriophage M13

Biochemistry ◽  
1996 ◽  
Vol 35 (32) ◽  
pp. 10383-10391 ◽  
Author(s):  
Ruud B. Spruijt ◽  
Cor J. A. M. Wolfs ◽  
Jan W. G. Verver ◽  
Marcus A. Hemminga
Keyword(s):  
Coat Protein ◽  
Transmembrane Domain ◽  
Cysteine Residues ◽  
Major Coat Protein ◽  
Putative Transmembrane Domain ◽  
Bacteriophage M13

scholarly journals Cysteine Residues in the Transmembrane Regions of M13 Procoat Protein Suggest that Oligomeric Coat Proteins Assemble onto Phage Progeny

2007 ◽  
Vol 189 (7) ◽  
pp. 2897-2905 ◽  
Author(s):  
Christof Nagler ◽  
Gisela Nagler ◽  
Andreas Kuhn
Keyword(s):  
Coat Protein ◽  
Leader Peptide ◽  
Cysteine Residues ◽  
Coat Proteins ◽  
Amino Acid Residues ◽  
Major Coat Protein ◽  
Phage Dna ◽  
Phage Assembly ◽  
Transmembrane Regions ◽  
Leader Peptidase

ABSTRACT The M13 phage assembles in the inner membrane of Escherichia coli. During maturation, about 2,700 copies of the major coat protein move from the membrane onto a single-stranded phage DNA molecule that extrudes out of the cell. The major coat protein is synthesized as a precursor, termed procoat protein, and inserts into the membrane via a Sec-independent pathway. It is processed by a leader peptidase from its leader (signal) peptide before it is assembled onto the phage DNA. The transmembrane regions of the procoat protein play an important role in all these processes. Using cysteine mutants with mutations in the transmembrane regions of the procoat and coat proteins, we investigated which of the residues are involved in multimer formation, interaction with the leader peptidase, and formation of M13 progeny particles. We found that most single cysteine residues do not interfere with the membrane insertion, processing, and assembly of the phage. Treatment of the cells with copper phenanthroline showed that the cysteine residues were readily engaged in dimer and multimer formation. This suggests that the coat proteins assemble into multimers before they proceed onto the nascent phage particles. In addition, we found that when a cysteine is located in the leader peptide at the −6 position, processing of the mutant procoat protein and of other exported proteins is affected. This inhibition of the leader peptidase results in death of the cell and shows that there are distinct amino acid residues in the M13 procoat protein involved at specific steps of the phage assembly process.

Role of Aromatic Residues at the Lipid−Water Interface in Micelle-Bound Bacteriophage M13 Major Coat Protein†

Biochemistry ◽  
2000 ◽  
Vol 39 (51) ◽  
pp. 16155-16162 ◽  
Author(s):  
Christopher T. K. Yuen ◽  
Alan R. Davidson ◽  
Charles M. Deber
Keyword(s):  
Coat Protein ◽  
Water Interface ◽  
Major Coat Protein ◽  
Aromatic Residues ◽  
Bacteriophage M13

scholarly journals NMR Studies of the Major Coat Protein of Bacteriophage M13. Structural Information of gVIIIp in Dodecylphosphocholine Micelles

1995 ◽  
Vol 232 (2) ◽  
pp. 490-500 ◽  
Author(s):  
Christina H. M. Papavoine ◽  
Jan M. A. Aelen ◽  
Ruud N. H. Konings ◽  
Cornelis W. Hilbers ◽  
Frank J. M. Ven
Keyword(s):  
Coat Protein ◽  
Structural Information ◽  
Nmr Studies ◽  
Major Coat Protein ◽  
Bacteriophage M13

Improving the copy numbers of antibody fragments expressed on the major coat protein of bacteriophage M13

1996 ◽  
Vol 2 (3) ◽  
pp. 197-207 ◽  
Author(s):  
Grace R. Nakayama ◽  
Gunars Valkirs ◽  
Diane McGrath ◽  
William D. Husea
Keyword(s):  
Coat Protein ◽  
Antibody Fragments ◽  
Major Coat Protein ◽  
Copy Numbers ◽  
Bacteriophage M13

scholarly journals Inserting foreign peptides into the major coat protein of bacteriophage M13

FEBS Letters ◽  
1992 ◽  
Vol 301 (3) ◽  
pp. 322-324 ◽  
Author(s):  
A.A. Ilyichev ◽  
O.O. Minenkova ◽  
G.P. Kishchenko ◽  
S.I. Tat'kov ◽  
N.N. Karpishev ◽  
...  
Keyword(s):  
Coat Protein ◽  
Major Coat Protein ◽  
Bacteriophage M13
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