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Association of Yeast SIN1 with the Tetratrico Peptide Repeats of CDC23
Sally Shpungin, Arthur Liberzon, Haim Bangio, Eyal Yona and Don J. Katcoff
Proceedings of the National Academy of Sciences of the United States of America
Vol. 93, No. 16 (Aug. 6, 1996), pp. 8274-8277
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/39851
Page Count: 4
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The yeast SIN1 protein is a nuclear protein that together with other proteins behaves as a transcriptional repressor of a family of genes. In addition, sin1 mutants are defective in proper mitotic chromosome segregation. In an effort to understand the basis for these phenotypes, we employed the yeast two-hybrid system to identify proteins that interact with SIN1 in vivo. Here we demonstrate that CDC23, a protein known to be involved in sister chromatid separation during mitosis, is able to directly interact with SIN1. Furthermore, using recombinant molecules in vitro, we show that the N terminal of SIN1 is sufficient to bind a portion of CDC23 consisting solely of tetratrico peptide repeats. Earlier experiments identified the C-terminal domain of SIN1 to be responsible for interaction with a protein that binds the regulatory region of HO, a gene whose transcription is repressed by SIN1. Taken together with the results presented here, we suggest that SIN1 is a chromatin protein having at least a dual function: The N terminal of SIN1 interacts with the tetratrico peptide repeat domains of CDC23, a protein involved in chromosome segregation, whereas the C terminal of SIN1 binds proteins involved in transcriptional regulation.
Proceedings of the National Academy of Sciences of the United States of America © 1996 National Academy of Sciences