TY - JOUR
T1 - DNA binding proteins in the cytoplasm of vaccinia virus infected mouse L cells
AU - Soloski, M. J.
AU - Esteban, M.
AU - Holowczak, J. A.
N1 - Copyright:
Copyright 2020 Elsevier B.V., All rights reserved.
PY - 1978
Y1 - 1978
N2 - Mouse L-cell fibroblasts were infected with vaccinia virus and labeled 2 to 3 h postinfection with [35S]methionine. Labeled proteins were fractionated on native and denatured DNA-cellulose columns and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Twenty-four vaccinia DNA-binding polypeptides (VDPs), ranging in molecular weight from 90,000 to 12,500, were detected. VDP-12A (molecular weight, 29,750) had affinity for denatured but not native DNA, and its sythesis was dependent on viral DNA replication. VDP-20 (molecular weight, 41,000) bound very tightly to native and denatured DNA and was displaced only after boiling the protein-DNA-cellulose matrix in 1% sodium dodecyl sulfate. VDP-8, -11, -12, -13, and -14 behaved electrophoretically like the polypeptide species previously shown to be present in DNA-protein complexes prepared from infected cells. The molecular weights of VDP-10 (50,000), VDP-11 (36,000), and VDP-8 (67,000) were similar to the polypeptide subunits of polyadenylate polymerase and phosphohydrolase I, enzymes purified from virions which have also been shown to have affinity for DNA.
AB - Mouse L-cell fibroblasts were infected with vaccinia virus and labeled 2 to 3 h postinfection with [35S]methionine. Labeled proteins were fractionated on native and denatured DNA-cellulose columns and then analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Twenty-four vaccinia DNA-binding polypeptides (VDPs), ranging in molecular weight from 90,000 to 12,500, were detected. VDP-12A (molecular weight, 29,750) had affinity for denatured but not native DNA, and its sythesis was dependent on viral DNA replication. VDP-20 (molecular weight, 41,000) bound very tightly to native and denatured DNA and was displaced only after boiling the protein-DNA-cellulose matrix in 1% sodium dodecyl sulfate. VDP-8, -11, -12, -13, and -14 behaved electrophoretically like the polypeptide species previously shown to be present in DNA-protein complexes prepared from infected cells. The molecular weights of VDP-10 (50,000), VDP-11 (36,000), and VDP-8 (67,000) were similar to the polypeptide subunits of polyadenylate polymerase and phosphohydrolase I, enzymes purified from virions which have also been shown to have affinity for DNA.
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U2 - 10.1128/jvi.25.1.263-273.1978
DO - 10.1128/jvi.25.1.263-273.1978
M3 - Article
C2 - 202739
AN - SCOPUS:0017836271
SN - 0022-538X
VL - 25
SP - 263
EP - 273
JO - Journal of virology
JF - Journal of virology
IS - 1
ER -