Synthesis and assembly of adenovirus type 2 polypeptides. II. Reversible inhibition of hexon assembly at 42 degrees. Academic Article

abstract

• Hexon polypeptides (monomers) synthesized at 42 do not assemble into capsomeres (trimers) until temperature stepdown to 37. Structural studies of monomer and trimer show them to be identical in molecular weight and tryptic peptide patterns. Cyanide and mercaptoethanol, both of which can interact with sulfhydryl groups, inhibit hexon assembly. Therefore, the oxidation state of each sulfhydryl group of cysteine was examined, but was found to be the same for free polypeptides and capsomeres. These observations suggest that factors other than the primary structure of the polypeptides are important for in vivo assembly. 1974.

authors

• Leibowitz, Julian

published proceedings

• Virology

author list (cited authors)

• Leibowitz, J., & Horwitz, M. S.

citation count

• 8

complete list of authors

• Leibowitz, J||Horwitz, MS

publication date

• September 1974

publisher

• Elsevier  Publisher

published in

• Virology  Journal

keywords

• Adenoviridae
• Amino Acids
• Carbon Radioisotopes
• Carcinoma
• Cell Fractionation
• Cell Line
• Cyanides
• Cycloheximide
• Depression, Chemical
• Electrophoresis, Polyacrylamide Gel
• Female
• Hela Cells
• Humans
• Mercaptoethanol
• Molecular Weight
• Mouth Neoplasms
• Peptide Biosynthesis
• Peptides
• Sulfur Radioisotopes
• Temperature
• Tritium
• Viral Proteins

PubMed Central ID

• 4416020

Digital Object Identifier (DOI)

• 10.1016/0042-6822(74)90248-7

start page

• 129

end page

• 139

volume

• 61

issue

• 1

URL

• http://dx.doi.org/10.1016/0042-6822(74)90248-7