Synthesis and assembly of adenovirus polypeptides. III. Reversible inhibition of hexon assembly in adenovirus type 5 temperature-sensitive mutants. Academic Article

abstract

• In cells infected with adenovirus type 5 temperature-sensitive mutants ts 17 and ts 20, hexon polypeptides (monomers) synthesized at 38.5 do not assemble into capsomeres (trimers) at that temperature. Although hexon polypeptides newly synthesized at the nonpermissive temperature assemble on temperature stepdown, holding the polypeptides at 38.5 for 2 hr before stepdown to 32.5 decreases assembly by 65-75%. Structural studies of wt and ts mutants have shown that the hexon polypeptides are identical in molecular weight, as well as tryptic and chymotryptic peptide patterns. These observations suggest that genes other than those coding for the primary structure of the hexon polypeptide are important for in vivo assembly of hexon. 1975.

authors

• Leibowitz, Julian

published proceedings

• Virology

author list (cited authors)

• Leibowitz, J., & Horwitz, M. S.

citation count

• 28

complete list of authors

• Leibowitz, J||Horwitz, MS

publication date

• July 1975

publisher

• Elsevier  Publisher

published in

• Virology  Journal

keywords

• Adenoviridae
• Carcinoma
• Cell Fractionation
• Cell Line
• Cyanides
• Cycloheximide
• Electrophoresis, Polyacrylamide Gel
• Hela Cells
• Humans
• Molecular Weight
• Mouth Neoplasms
• Mutation
• Nitrates
• Peptide Biosynthesis
• Temperature
• Viral Proteins

PubMed Central ID

• 1136138

Digital Object Identifier (DOI)

• 10.1016/0042-6822(75)90175-0

start page

• 10

end page

• 24

volume

• 66

issue

• 1

URL

• http://dx.doi.org/10.1016/0042-6822(75)90175-0