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| PACKING OF COAT PROTEIN AMPHIPATHIC AND TRANSMEMBRANE HELICES IN FILAMENTOUS BACTERIOPHAGE-M13 - ROLE OF SMALL RESIDUES IN PROTEIN OLIGOMERIZATION |
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| Author(s): WILLIAMS KA, GLIBOWICKA M, LI ZM, LI H, KHAN AR, CHEN YMY, WANG J, MARVIN DA, DEBER CM |
| Source: JOURNAL OF MOLECULAR BIOLOGY Volume: 252 Issue: 1 Pages: 6-14 Published: SEP 8 1995 |
| Times Cited: 50 References: 31 |
| Abstract: Filamentous bacteriophage M13, an important cloning and phage display vector, is encapsulated by ca 2700 copies of its 50-residue major coat protein (gene 8). This protein occurs as a membrane protein while stably inserted into its E. coli host inner membrane, and as a coat protein upon assembly and packing onto phage DNA in the lipid-free virion. To examine the specific protein-protein interactions underlying these processes, we used a combination of randomized and saturation mutagenesis of the entire gene 8 to assess the susceptibility of each position to mutation. In the resulting library of ca 100 viable M13 mutants, ''small'' residues (Ala, Gly, Ser), which constitute the non-polar face of the N-terminal amphipathic helical segment, and a face of the hydrophobic (effective transmembrane) helical segment, were found to be highly conserved. These results support a model in which coat protein packing is stabilized by the presence within each protein subunit of two ''oligomerization segments'' i.e. specific helical regions with faces rich in small residues which function to promote the close approach of alpha-helices. (C) 1995 Academic Press Limited |
| Document Type: Note |
| Language: English |
Addresses:
1. HOSP SICK CHILDREN, RES INST, DIV BIOCHEM, TORONTO, ON M5G 1X8 CANADA
2. UNIV TORONTO, DEPT BIOCHEM, TORONTO, ON M5S 1A8 CANADA
3. NATL RES COUNCIL CANADA, BIOTECHNOL RES INST, MONTREAL, PQ H4P 2R2 CANADA
4. UNIV CAMBRIDGE, DEPT BIOCHEM, CAMBRIDGE CB2 1QW, ENGLAND |
| Publisher: ACADEMIC PRESS (LONDON) LTD, 24-28 OVAL RD, LONDON, ENGLAND NW1 7DX |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: RT965 |
| ISSN: 0022-2836 |
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