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Published October 22, 1993 | public
Journal Article

A yeast protein similar to bacterial two-component regulators


Many bacterial signaling pathways involve a two-component design. In these pathways, a sensor kinase, when activated by a signal, phosphorylates its own histidine, which then serves as a phosphoryl donor to an aspartate in a response regulator protein. The Sln1 protein of the yeast Saccharomyces cerevisiae has sequence similarities to both the histidine kinase and the response regulator proteins of bacteria. A missense mutation in SLN1 is lethal in the absence but not in the presence of the N-end rule pathway, a ubiquitin-dependent proteolytic system. The finding of SLN1 demonstrates that a mode of signal transduction similar to the bacterial two-component design operates in eukaryotes as well.

Additional Information

© 1993 American Association for the Advancement of Science. July 1993; Accepted 22 September 1993. We thank E. Meyerowitz, C. Chang, M. Simon, and L. Alex for sharing unpublished results; L. Riles for Prime Clone Blots; members of the laboratory for helpful discussions and advice; and C. Byrd, T. Clandinin, E. Johnson, N. Johnsson, F. Lévy, and K. Madura for comments on the manuscript. Supported by grants to A.V. from the National Institutes of Health.

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