E3-ubiquitin ligase/E6-AP links multicopy maintenance protein 7 to the ubiquitination pathway by a novel motif, the L2G box.

Ubiquitin ligases are generally assumed to play a major role in substrate recognition and thus provide specificity to a particular ubiquitin modification system. The multicopy maintenance protein (Mcm) 7 subunit of the replication licensing factor-M was identified as a substrate of the E3-ubiquitin ligase/E6-AP by its interaction with human papillomavirus-18E6. ...
Mcm7 is ubiquitinated in vivo in both an E6-AP-dependent and -independent manner. E6-AP functions in these reactions independently of the viral oncogene E6. We show that recognition of Mcm7 by E6-AP is mediated by a homotypic interaction motif present in both proteins, called the L2G box. These findings served as the basis for the definition of substrate specificity for E6-AP. A small cluster of proteins whose function is intimately associated with the control of cell growth and/or proliferation contains the L2G box and is thereby implicated in an E6-AP and, by default, HPV-E6-dependent ubiquitination pathway.
Mesh Terms:
Amino Acid Sequence, Antibodies, Cell Cycle Proteins, Conserved Sequence, DNA Primers, DNA Replication, DNA-Binding Proteins, Hela Cells, Humans, Ligases, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligodeoxyribonucleotides, Papillomaviridae, Peptide Fragments, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity, Ubiquitin-Protein Ligases, Ubiquitins
J. Biol. Chem.
Date: Dec. 18, 1998
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