Interaction between the gene 5 protein, gene 5 protein/single stranded fd DNA complex and gene 8 protein of the filamentous phage fd

Boehler-Kohler, Beverly A.; Rasched, Ihab

doi:10.1016/0006-291x(87)91598-1

Cited by 3 publications

(1 citation statement)

References 21 publications

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“…Therefore, the -helical state is thought to be effective in the assembly process. This is in agreement with the previously presented idea of monomeric coat protein insertion and processing of newly synthesized coat protein (Kuhn et al, 1986), the exchange interaction between gene V proteins and monomeric coat protein on the viral DNA (Boehler-Kohler & Rasched, 1987), and the commonly accepted idea that parental coat protein can be re-used in the assembly process (Armstrong et al, 1983), indicating reversible uncoating and encapsulating processes.…”

Section: Resultssupporting

confidence: 92%

The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli

Spruijt¹,

Hemminga²

1991

Biochemistry

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The major coat protein of bacteriophage M13 has been reconstituted into phospholipids with a composition comparable to that found in the host (Escherichia coli) inner membrane. Reconstitution experiments have revealed conditions in which the alpha-oligomeric state is favored over the beta-polymeric state. Discrimination between the two states of the membrane-bound coat protein (alpha-oligomeric and beta-polymeric states) has been achieved using high-performance size-exclusion chromatography and circular dichroism. Interprotein electrostatic interactions, probably induced by head-tail binding, are initiated and facilitating the aggregation-related conformational change process, in which alpha-oligomeric coat protein is converted into beta-polymeric coat protein. A model for this beta-polymerization process of the coat protein is presented. The alpha-helical protein has been studied by the in situ Trp fluorescence quantum yield. This shows that the average distances between coat proteins decrease upon lowering the L/P ratio. In situ cross-linking reactions of the coat protein at high L/P ratios reveal a monomeric state, thus excluding specific aggregation of the coat protein. A monomeric state of detergent-solubilized coat protein is also observed using SDS-PAGE and SDS-HPSEC. On the basis of these results, the smallest in situ aggregational entity of the coat protein is proposed to be a monomer. This finding is discussed in relation to the functional state of the M13 coat protein in the membrane-bound assembly and disassembly processes during infection.

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Section: Resultssupporting

confidence: 92%

The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli

Spruijt¹,

Hemminga²

1991

Biochemistry

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Chapter 8 Lipid-protein interactions involved in bacteriophage M13 infection

Hemminga

Sanders

Wolfs

et al. 1993

Protein-Lipid Interactions

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Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13

Spruijt¹,

Wolfs²,

Hemminga³

1989

Biochemistry

122

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The state of the coat protein of bacteriophage M13, reconstituted into amphiphilic media, has been investigated. The in situ conformation of the coat protein has been determined by using circular dichroism. Minimum numbers for the protein aggregation in the system have been determined after disruption of the lipid-protein system and subsequent uptake of the protein in cholate micelles. The aggregational state and conformation of the protein were affected by (1) the method of coat protein isolation (phenol extraction vs cholate isolation), (2) the nature of amphiphiles used (variation in phospholipid headgroups and acyl chains), and (3) the ratio of amphiphiles and protein. Under all conditions, phenol-extracted coat protein was in a predominantly beta-structure and in a highly aggregated polymeric form. Cholate-isolated coat protein was initially oligomeric and contained a substantial amount of alpha-helix. Below an aggregation number of 20, this protein showed a reversible aggregation with no change in conformation. Upon further aggregation, a conformational change was observed, and aggregation was irreversible, resulting in predominantly beta-structured coat protein polymers. This effect was observed upon uptake in phospholipids at low lipid to protein molar ratios (L/P ratios) and with phosphatidylcholines (PC) and phosphatidic acids (PA) containing saturated acyl chains. After reconstitution in phospholipids with unsaturated acyl chains and with phosphatidylglycerols (PG) at high L/P ratios, the original alpha-helix-containing state of the coat protein was maintained. Cross-linking experiments demonstrated that the beta-polymers are able to form reversible superaggregates within the vesicle system. An aggregation-related conformational change mechanism for the coat protein in phospholipid systems is proposed.

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Interaction between the gene 5 protein, gene 5 protein/single stranded fd DNA complex and gene 8 protein of the filamentous phage fd

Cited by 3 publications

References 21 publications

The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli

The in situ aggregational and conformational state of the major coat protein of bacteriophage M13 in phospholipid bilayers mimicking the inner membrane of host Escherichia coli

Chapter 8 Lipid-protein interactions involved in bacteriophage M13 infection

Aggregation-related conformational change of the membrane-associated coat protein of bacteriophage M13

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