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P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly
- Source :
- Journal of supramolecular structure. 2(2-4)
- Publication Year :
- 1974
-
Abstract
- 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.
- Subjects :
- Scaffold protein
Salmonella typhimurium
Time Factors
Macromolecular Substances
Ultraviolet Rays
Biology
DNA condensation
Cleavage (embryo)
Virus Replication
chemistry.chemical_compound
Viral Proteins
Centrifugation, Density Gradient
Morphogenesis
Carbon Radioisotopes
Prohead
General Medicine
Electrophoresis, Disc
Macromolecular assembly
Molecular Weight
Radiation Effects
Microscopy, Electron
Capsid
Biochemistry
chemistry
Genes
Isotope Labeling
DNA, Viral
Mutation
Biophysics
Salmonella Phages
DNA
Subjects
Details
- ISSN :
- 00917419
- Volume :
- 2
- Issue :
- 2-4
- Database :
- OpenAIRE
- Journal :
- Journal of supramolecular structure
- Accession number :
- edsair.doi.dedup.....e79aba41873abc77f0ace05c9d814d77