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Published October 22, 1993 | public
Journal Article

A yeast protein similar to bacterial two-component regulators

Abstract

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 We thank E. Meyerowitz, C. Chang, M. Simon, and L. Alex for sharing unpublished results; L. Riles for Prime Clone Blots; members of the laboratory for helpful discussions and advice; and C. Byrd, T. Clandinin, E. Johnson, N. Johnsson, F.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.

Additional details

Created:
August 20, 2023
Modified:
October 19, 2023