TY - JOUR
T1 - The structure of nucleoprotein cores released from adenovirions
AU - Vayda, Michael E.
AU - Rogers, Alan E.
AU - Flint, S. J.
N1 - Funding Information:
We thank M. Hogan for helpful discussions and critical comments on this work. We are grateful to M. Young, M.E. Steele and M. Vanek for excellent technical assistance and to R. Pastori and N. Mann for preparation of the manuscript. This work was supported by a grant from the American Cancer Society, #NP239C and M.E.V. by a PHS training Grant, 0GMO7388.
PY - 1983/1/25
Y1 - 1983/1/25
N2 - The morphology, protein composition and DNA organization of nucleoprotein core complexes isolated from type 5 adenovirions have been examined by electron microscopy and biochemical techniques. The morphology of such core structures is in some ways strikingly similar to that exhibited by cellular chromatin. 'Native' core preparations contain compact and less highly-folded forms: the latter appear as thick fibres, 150-300Å in diameter. Upon exposure to 0.4M NaC1, adenovirus cores undergo a transition to a beaded string form, reminiscent of nucleosomes. Of the three arginine-rich proteins, polypeptides V, VII and μ present in 'native' cores, only polypeptide VII remains associated with viral DNA in the presence of 0.4M NaC1. We therefore conclude that the nucleosome-like beads are constructed solely of polypeptide VII. The results of micrococcal nuclease digestion experiments suggest that polypeptide VII is sufficient to protect some 100-300bp of adenoviral DNA.
AB - The morphology, protein composition and DNA organization of nucleoprotein core complexes isolated from type 5 adenovirions have been examined by electron microscopy and biochemical techniques. The morphology of such core structures is in some ways strikingly similar to that exhibited by cellular chromatin. 'Native' core preparations contain compact and less highly-folded forms: the latter appear as thick fibres, 150-300Å in diameter. Upon exposure to 0.4M NaC1, adenovirus cores undergo a transition to a beaded string form, reminiscent of nucleosomes. Of the three arginine-rich proteins, polypeptides V, VII and μ present in 'native' cores, only polypeptide VII remains associated with viral DNA in the presence of 0.4M NaC1. We therefore conclude that the nucleosome-like beads are constructed solely of polypeptide VII. The results of micrococcal nuclease digestion experiments suggest that polypeptide VII is sufficient to protect some 100-300bp of adenoviral DNA.
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U2 - 10.1093/nar/11.2.441
DO - 10.1093/nar/11.2.441
M3 - Article
C2 - 6828374
AN - SCOPUS:0021111527
SN - 0305-1048
VL - 11
SP - 441
EP - 460
JO - Nucleic acids research
JF - Nucleic acids research
IS - 2
ER -