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  • 1
    Electronic Resource
    Electronic Resource
    Assembly of the tail of bacteriophage T4 (1975)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 24-38 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The protein products of at least 21 phage genes are needed for the formation of the tail of bacteriophage T4. Cells infected with amber mutants defective in these genes are blocked in the assembly process. By characterizing the intermediate structures and unassembled proteins accumulating in mutant-infected cells, we have been able to delineate most of the gene-controlled steps in tail assembly. Both the organized structures and unassembled proteins serve as precursors for in vitro tail assembly.We review here studies on the initiation, polymerization, and termination of the tail tube and contractile sheath and the genetic control of these processes. These studies make clear the importance of the baseplate; if baseplate formation is blocked (by mutation) the tube and sheath subunits remain essentially unaggregated, in the form of soluble subunits.Seventeen of the 21 tail genes specify proteins involved in baseplate assembly. The genes map contiguously in two separate clusters, one of nine genes and the other of eight genes. Recent studies show that the hexagonal baseplate is the end-product of two independent subassembly pathways. The proteins of the first gene cluster interact to form a structure which probably represents one-sixth of the outer radius. The products of the other gene cluster interact to form the central part of the baseplate.Most of the phage tail precursor proteins appear to be synthesized in a non-aggregating form; they are converted to a reactive form upon incorporation into preformed substrate complexes, without proteolytic cleavage. Thus reactive sites are limited to growing structures.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400030104
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    P22 morphogenesis I: Catalytic scaffolding protein in capsid assembly (1974)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 2 (1974), S. 202-224 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: About 250 molecules of the 42,000 molecular weight gene 8 product catalyze the polymerization of the major phage coat protein into a precursor shell temporarily containing both proteins. The resulting prohead appears to be a shell structure with the P8, or scaffolding protein, on the inside, and the coat protein on the outside. In concert with DNA condensation inside the shell, all 250 scaffolding molecules exit from the prohead, without proteolytic cleavage. These molecules then recycle and catalyze the formation of more proheads from newly synthesized coat protein. Such proteins, which catalyze assembly by temporarily associating with an intermediate stage, may represent a general mechanism of macromolecular assembly.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400020215
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    Paper (German National Licenses)
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