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Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.

Acta biochimica Polonica - 1 Jan 2005

Kamińska Joanna, Kwapisz Marta, Grabińska Kariona, Orłowski Jacek, Boguta Magdalena, Palamarczyk Grazyna, Zoładek Teresa

Abstract excerpt

Dimethylallyl diphosphate, an isomer of isopentenyl diphosphate, is a common substrate of Mod5p, a tRNA modifying enzyme, and the farnesyl diphosphate synthase Erg20p, the key enzyme of the isoprenoid pathway. rsp5 mutants, defective in the Rsp5 ubiquitin-protein ligase, were isolated and characterized as altering the mitochondrial/cytosolic distribution of Mod5p. To understand better how competition for the...

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PMID: 15827618

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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