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Mdm30p, an F‐box protein, stimulates export of mRNA in vivo.
Author(s) -
Shukla Abhijit,
Schneider Jessica,
Shadle Thomas,
Bajwa Pratibha,
Shilatifard Ali,
Bhaumik Sukesh
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a656-d
Subject(s) - messenger rna , microbiology and biotechnology , gene expression , rna polymerase ii , biology , ubiquitin , in vivo , gene , chemistry , biochemistry , genetics , promoter
Mdm30p, an F‐box protein which binds substrate for ubiquitin‐mediated proteolysis, is required for maintenance of fusion‐competent mitochondria. Recently, Mdm30p has been implicated in regulation of gene expression. However, the mechanism‐of‐action of Mdm30p in gene regulation remains largely unknown in vivo . Here, using a formaldehyde‐based in vivo cross‐linking and chromatin immunoprecipitation assay, we show that Mdm30p is dispensable for formation of the preinitiation complex assembly and recruitment of mRNA capping enzyme, cap‐binding complex, elongating RNA polymerase II and mRNA 3′‐end formation machinery at a transcriptionally active gene, ADH1 . Interestingly, recruitment of mRNA export machinery at ADH1 is greatly reduced in Δ mdm30 . Consistently, export of ADH1 mRNA is significantly impaired in the absence of Mdm30p. Thus, our data reveal that Mdm30p is selectively required for recruitment of mRNA export machinery (and hence mRNA export) at the active gene in vivo, demonstrating a new role of an F‐box protein in regulation of mRNA export.