A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

Article Abstract:

A glycolytic enzyme, enolase, is identified as a factor of tRK1 import in Saccharomyces cerevisiae and the recombination enolase and preMSK1p which are sufficient to direct RNA import in vitro is demonstrated and depletion of enolase inhibits tRNA import in vivo. A model suggesting that the cell exploits mitochonrial targeting of the enolase in order to address the tRNA toward peri-mitochondrically synthesized preMsk1p is proposed.

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Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae

Article Abstract:

The subunits shared by SWRI-Com and NuA4 leads to the test whether H2A.Z in Saccharomyces cerevisiae, a substrate for SWR1-Com, is also a substrate for NuA4. The results suggest that unacetylatable H2A.Z mutants are, like wild-type H2A.Z, enriched at heterochromatin boundaries, but are unable to block spreading of heterochromatin.

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SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in Saccharomyces cerevisiae

Article Abstract:

The yeast SAS (Something About Silencing) is an H4 Lys 16-specific histone acetyltransferase complex. A demonstration that the H4 Lys 16 acetylation by SAS is required for efficient H2A is presented.

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