Open AccessP22 morphogenesis I: Catalytic scaffolding protein in capsid assembly
Author(s) -
Casjens Sherwood,
King Jonathan
Publication year - 1974
Publication title -
journal of supramolecular structure
Language(s) - English
Resource type - Journals
eISSN - 1547-9366
pISSN - 0091-7419
DOI - 10.1002/jss.400020215
Subject(s) - capsid , scaffold protein , chemistry , scaffold , cleavage (geology) , macromolecule , biophysics , dna , molecule , polymerization , microbiology and biotechnology , biochemistry , gene , biology , polymer , organic chemistry , medicine , paleontology , signal transduction , fracture (geology) , biomedical engineering
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.