NDLI: Cycloheximide resistance conferred by novel mutations in ribosomal protein L41 of Chlamydomonas reinhardtii

Content Provider	Springer Nature Link
Author	Stevens, D. R. Atteia, A. Franzén, L. G. Purton, S.
Copyright Year	2000
Abstract	Although most eukaryotic cells are sensitive to the 80S ribosome inhibitor cycloheximide (CYH), naturally occurring CYH resistance is widespread amongst yeast species. The primary determinant of resistance appears to be a single residue within ribosomal protein L41; resistance is acquired by the substitution of a conserved proline (P56) by a glutamate residue. We have isolated the L41 gene (RPL41) from the green alga Chlamydomonas reinhardtii, and investigated the molecular basis of CYH resistance in various mutant strains. In both the wild-type strain and the mutant act-1, a proline is found at the key position in L41. However, analysis of six independently isolated act-2 mutants reveals that all have point mutations that replace the proline with either leucine or serine. Of the two changes, the leucine mutation confers significantly higher levels of CYH resistance. This work identifies the ACT-2 locus as RPL41 and provides a possible dominant marker for nuclear transformation of C. reinhardtii.
Starting Page	790
Ending Page	795
Page Count	6
File Format	PDF
ISSN	00268925
Journal	Molecular and General Genetics MGG
Volume Number	264
Issue Number	6
e-ISSN	14321874
Language	English
Publisher	Springer-Verlag
Publisher Date	2000-10-25
Publisher Place	Berlin/Heidelberg
Access Restriction	Subscribed
Content Type	Text
Resource Type	Article
Subject	Genetics

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