Characterization of the adenovirus 2 virion protein, Mu

Carl W. Anderson; Marjorie E. Young; S. J. Flint

doi:10.1016/0042-6822(89)90193-1

Characterization of the adenovirus 2 virion protein, Mu

Carl W. Anderson
, Marjorie E. Young
, S. J. Flint

Molecular Biology

Research output: Contribution to journal › Article › peer-review

71 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	506-512
Number of pages	7
Journal	Virology
Volume	172
Issue number	2
DOIs	https://doi.org/10.1016/0042-6822(89)90193-1
State	Published - Oct 1989

All Science Journal Classification (ASJC) codes

Virology

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10.1016/0042-6822(89)90193-1

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@article{97d6a9be7c5441daa40fbd1979fcbfcd,

title = "Characterization of the adenovirus 2 virion protein, Mu",

abstract = "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.",

author = "Anderson, \{Carl W.\} and Young, \{Marjorie E.\} and Flint, \{S. J.\}",

note = "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 .",

year = "1989",

month = oct,

doi = "10.1016/0042-6822(89)90193-1",

language = "English (US)",

volume = "172",

pages = "506--512",

journal = "Virology",

issn = "0042-6822",

publisher = "Academic Press Inc.",

number = "2",

}

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 - https://www.scopus.com/pages/publications/0024326120

UR - https://www.scopus.com/pages/publications/0024326120#tab=citedBy

U2 - 10.1016/0042-6822(89)90193-1

DO - 10.1016/0042-6822(89)90193-1

M3 - Article

C2 - 2800334

AN - SCOPUS:0024326120

SN - 0042-6822

VL - 172

SP - 506

EP - 512

JO - Virology

JF - Virology

IS - 2

ER -

Characterization of the adenovirus 2 virion protein, Mu

Abstract

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