Dataset Information

Identification of multiple CDH1 homologues in vertebrates conferring different substrate specificities.

ABSTRACT: CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1). We have found multiple functional CDH1 homologues in the chick. The transcripts of these novel genes are differentially localized to proliferating, differentiated, and postmitotic tissues. All four proteins bind and form a complex with APC in vitro and in cultural cells and have quantitatively different activities in mediating ubiquitination of various APC substrates. Our results suggest that multiple CDH1s may temporally and spatially regulate APC activity both within and outside of the cell cycle.

SUBMITTER: Wan Y

PROVIDER: S-EPMC60825 | biostudies-literature | 2001 Nov

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Identification of multiple CDH1 homologues in vertebrates conferring different substrate specificities.

Wan Y Y Kirschner M W MW

Proceedings of the National Academy of Sciences of the United States of America 20011030 23

CDC20/CDH1 activates the anaphase-promoting complex (APC) and targets various substrates for degradation, thereby allowing the ordered progression through mitosis and G(1). We have found multiple functional CDH1 homologues in the chick. The transcripts of these novel genes are differentially localized to proliferating, differentiated, and postmitotic tissues. All four proteins bind and form a complex with APC in vitro and in cultural cells and have quantitatively different activities in mediatin ...[more]

PMID: 11687641

Similar Datasets

Project description:Polycomb group (PcG) proteins maintain expression pattern of genes set early during development. Although originally isolated as regulators of homeotic genes, PcG members play a key role in epigenetic mechanism that maintains the expression state of a large number of genes. Polycomb (PC) is conserved during evolution and while invertebrates have one PC gene, vertebrates have five or more homologues. It remains unclear if different vertebrate PC homologues have distinct or overlapping functions. We have identified and compared the sequence of PC homologues in various organisms to analyze similarities and differences that shaped the evolutionary history of this key regulatory protein.All PC homologues have an N-terminal chromodomain and a C-terminal Polycomb Repressor box. We searched the protein and genome sequence database of various organisms for these signatures and identified approximately 100 PC homologues. Comparative analysis of these sequences led to the identification of a novel insect specific motif and several novel and signature motifs in the vertebrate homologue: two in CBX2 (Cx2.1 and Cx2.2), four in CBX4 (Cx4.1, Cx4.2, Cx4.3 and Cx4.4), three in CBX6 (Cx6.1, Cx6.2 and Cx6.3) and one in CBX8 (Cx8.1). Additionally, adjacent to the chromodomain, all the vertebrate homologues have a DNA binding motif - AT-Hook in case of CBX2, which was known earlier, and 'AT-Hook Like' motif, from this study, in other PC homologues.Our analysis shows that PC is an ancient gene dating back to pre bilaterian origin that has not only been conserved but has also expanded during the evolution of complexity. Unique motifs acquired by each homologue have been maintained for more than 500 millions years indicating their functional relevance in boosting the epigenetic 'tool kit'. We report the presence of a DNA interaction motif adjacent to chromodomain in all vertebrate PC homologues and suggest a three-way 'PC-histoneH3-DNA' interaction that can restrict nucleosome dynamics. The signature motifs of PC homologues and insect specific motif identified in this study pave the way to understand the molecular basis of epigenetic mechanisms.

Dataset Information

Identification of multiple CDH1 homologues in vertebrates conferring different substrate specificities.

Publications

Identification of multiple CDH1 homologues in vertebrates conferring different substrate specificities.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure