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Article

A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations.

Journal of biochemistry - 1 Mar 2004

Okano Hiroyuki, Asakawa Masayo, Ohya Yoshikazu

Abstract excerpt

Calmodulin (CaM) performs essential functions in cell proliferation in Saccharomyces cerevisiae. Previously, we isolated fourteen temperature-sensitive Phe-to-Ala mutations of the CaM-encoding gene CMD1. These mutations were classified into four intragenic complementation groups, suggesting that each group represents a loss of CaM interaction with its specific essential target protein. Nuf1p/Spc110p, one of the...

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PMID: 15113827
DOI: 10.1093/jb/mvh035

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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A novel mechanism of intragenic complementation between Phe to Ala calmodulin mutations.PMID 15113827Read ↗

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