Abstract
We recently reported that the 'hydrophobic patch' (HP) of the Saccharomyces cerevisiae S-phase cyclin Clb5 facilitates its interaction with Orc6 (via its Cy or RXL motif), providing a mechanism that helps prevent rereplication from individual origins. This is the first finding of a biological function for an interaction between a cyclin and a cyclin-binding motif (Cy or RXL motif) in a target protein in Saccharomyces cerevisiae. It is also the first such example involving a B-type cyclin in any organism. Yet, some of our observations as well as work from other groups suggest that HP-RXL interactions are functionally important for cyclin-Cdk signaling to other targets. The evolutionary conservation of the HP motif suggests that it allows cyclins to carry out important and specialized functions.
MeSH terms
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Amino Acid Motifs
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Amino Acid Sequence
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Cell Cycle / genetics
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Cell Cycle / physiology
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Cyclin B / chemistry
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Cyclin B / genetics
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Cyclin B / physiology*
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Cyclin-Dependent Kinases / genetics
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Cyclin-Dependent Kinases / physiology
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Cyclins / genetics
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Cyclins / physiology
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DNA Replication
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Gene Expression Regulation, Fungal*
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Hydrophobic and Hydrophilic Interactions
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Molecular Sequence Data
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Origin Recognition Complex / chemistry
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Origin Recognition Complex / genetics
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Origin Recognition Complex / physiology*
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Protein Structure, Tertiary
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / physiology*
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Saccharomyces cerevisiae Proteins / chemistry
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / physiology*
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Signal Transduction / genetics
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Signal Transduction / physiology
Substances
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CLB5 protein, S cerevisiae
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Cyclin B
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Cyclins
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ORC6 protein, S cerevisiae
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Origin Recognition Complex
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Saccharomyces cerevisiae Proteins
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Cyclin-Dependent Kinases