TY - JOUR
T1 - Characterization of the adenovirus 2 virion protein, Mu
AU - Anderson, Carl W.
AU - Young, Marjorie E.
AU - Flint, S. J.
N1 - Funding Information:
We are grateful to D . Marshak, Cold Spring Harbor Laboratory, for the time-of-flight mass analysis performed on the BI0-ION 20 mass spectrometer, and to M . Flocco, Princeton University, for preparation of the synthetic mu peptide . We also thank R . Greene, N . Alonzo, J . Wysocki, and S . Lamb for excellent technical assistance . This research was sponsored in part by Contract U01 A126049 from the National Institutes of Health to C .W .A . and by Grant Al 24545 from the National Institutes of Health to S .J .F . C .W .A . is supported in part by the Office of Health and Environmental Research of the U .S . Department of Energy .
PY - 1989/10
Y1 - 1989/10
N2 - Adenovirus 2 virions contain a small, highly basic protein known as μ (mu). Partial sequence analysis of mu labeled with radioactive amino acids showed that it is derived from an 11-kDa virion precursor protein, L2-79R. Amino acid analysis, direct microsequence analysis, time-of-flight mass spectrometer analysis, and chemical synthesis demonstrated that mu is the unmodified, 19 amino acid peptide obtained from the 79-residue precursor by adenovirus-encoded proteinase-mediated cleavage after glycine31 and glycine50. Mu bound tightly to DNA and was located in the virion core. In vitro, mu could precipitate DNA fragments, suggesting that it may have a role in viral chromosome condensation.
AB - Adenovirus 2 virions contain a small, highly basic protein known as μ (mu). Partial sequence analysis of mu labeled with radioactive amino acids showed that it is derived from an 11-kDa virion precursor protein, L2-79R. Amino acid analysis, direct microsequence analysis, time-of-flight mass spectrometer analysis, and chemical synthesis demonstrated that mu is the unmodified, 19 amino acid peptide obtained from the 79-residue precursor by adenovirus-encoded proteinase-mediated cleavage after glycine31 and glycine50. Mu bound tightly to DNA and was located in the virion core. In vitro, mu could precipitate DNA fragments, suggesting that it may have a role in viral chromosome condensation.
UR - http://www.scopus.com/inward/record.url?scp=0024326120&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0024326120&partnerID=8YFLogxK
U2 - 10.1016/0042-6822(89)90193-1
DO - 10.1016/0042-6822(89)90193-1
M3 - Article
C2 - 2800334
AN - SCOPUS:0024326120
VL - 172
SP - 506
EP - 512
JO - Virology
JF - Virology
SN - 0042-6822
IS - 2
ER -