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J. Biol. Chem., Vol. 269, Issue 42, 26539-26545, Oct, 1994
C Ptak, JA Prendergast, R Hodgins, CM Kay, V Chau and MJ Ellison
Like several other ubiquitin-conjugating enzymes, the yeast cell cycle
enzyme CDC34 (UBC3) has a carboxyl-terminal extension or tail. These tails
appear to carry out unique functions that can vary from one
ubiquitin-conjugating enzyme to the next. Using biophysical techniques we
have determined that the tail of CDC34 constitutes a highly structured and
extended domain. Although the tail of CDC34 is the largest tail identified
to date (125 residues), we have found that only 39 residues lying adjacent
to the catalytic domain are necessary and sufficient for full cell cycle
function and that this region fulfills a novel function that may be common
to the tails of other ubiquitin- conjugating enzymes. Cross-linking studies
demonstrate that this region facilitates a physical interaction between
CDC34 monomers in vitro. Furthermore, phenotypic analysis of various CDC34
derivatives expressed in different cdc34 mutant strains indicates that this
region facilitates the same interaction in vivo. Based on these findings,
it appears that the cell cycle function of CDC34 is dependent upon the
ability of CDC34 monomers to interact with one another and that this
interaction is mediated by a small region of the CDC34 tail. The similarity
of this region with sequences contained within the tails of the UBC1 and
UBC6 enzymes suggests that these tails may function in a similar manner.
Functional and physical characterization of the cell cycle ubiquitin- conjugating enzyme CDC34 (UBC3). Identification of a functional determinant within the tail that facilitates CDC34 self-association
Department of Biochemistry, University of Alberta, Edmonton, Canada.
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