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J Biol Chem, Vol. 273, Issue 51, 34302-34309, December 18, 1998
From the International Centre for Genetic Engineering and
Biotechnology, Padriciano 99, I-34012 Trieste, Italy
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.
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