Interaction Between Human Cyclin A and Adenovirus E1A-Associated p107 Protein

The products of the adenovirus early region 1A (E1A) gene are potent oncoproteins when tested in standard transformation and immortalization assays. Many of the changes induced by E1A may be due to its interaction with cellular proteins. Four of these cellular proteins are the retinoblastoma protein...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1992-01, Vol.255 (5040), p.87-90
Main Authors: Faha, Barbara, Ewen, Mark E., Tsai, Li-Huei, Livingston, David M., Harlow, Ed
Format: Article
Language:English
Subjects:
adenovirus
Adenovirus Early Proteins
Adenoviruses
Amino Acid Sequence
Amino acids
Antibodies
Antibodies, Monoclonal
CDC2 Protein Kinase - metabolism
Cell cycle
Cell Line
Cell lines
Cellular biology
Coding
Cyclins
Cyclins - immunology
Cyclins - isolation & purification
Cyclins - metabolism
Electrophoresis, Polyacrylamide Gel
Gels
Genetics
Glutathione Transferase - genetics
Glutathione Transferase - isolation & purification
Humans
Methionine - metabolism
Molecular Sequence Data
Myeloid leukemia
Nuclear Proteins
Oncogene Proteins, Viral - metabolism
Protein binding
Proteins
Proteins - genetics
Proteins - metabolism
Recombinant Fusion Proteins - isolation & purification
Retinoblastoma Protein - metabolism
Retinoblastoma-Like Protein p107
Transcription factors
Viral tumor antigens
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Summary:The products of the adenovirus early region 1A (E1A) gene are potent oncoproteins when tested in standard transformation and immortalization assays. Many of the changes induced by E1A may be due to its interaction with cellular proteins. Four of these cellular proteins are the retinoblastoma protein (pRB), p107, cyclin A, and p33$^{cdk2}$. The pRB and p107 proteins are structurally related and have several characteristics in common, including that they both bind to the SV40 large T oncoprotein as well as to E1A. Cyclin A and p33$^{cdk2}$ are thought to function in the control of the cell cycle. They bind to one another, forming a kinase that closely resembles the cell cycle-regulating complexes containing p34$^{cdc2}$. Cyclin A is now shown to bind to p107 in the absence of E1A. The association of p107 with cyclin A suggests a direct link between cell cycle control and the function of p107.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1532458