title: Functional interactions between yeast mitochondrial ribosomes and mRNA 5' untranslated leaders.
abstract: Translation of mitochondrial mRNAs in Saccharomyces cerevisiae depends on mRNA-specific translational activators that recognize the 5' untranslated leaders (5'-UTLs) of their target mRNAs. We have identified mutations in two new nuclear genes that suppress translation defects due to certain alterations in the 5'-UTLs of both the COX2 and COX3 mRNAs, indicating a general function in translational activation. One gene, MRP21, encodes a protein with a domain related to the bacterial ribosomal protein S21 and to unidentified proteins of several animals. The other gene, MRP51, encodes a novel protein whose only known homolog is encoded by an unidentified gene in S. kluyveri. Deletion of either MRP21 or MRP51 completely blocked mitochondrial gene expression. Submitochondrial fractionation showed that both Mrp21p and Mrp51p cosediment with the mitochondrial ribosomal small subunit. The suppressor mutations are missense substitutions, and those affecting Mrp21p alter the region homologous to E. coli S21, which is known to interact with mRNAs. Interactions of the suppressor mutations with leaky mitochondrial initiation codon mutations strongly suggest that the suppressors do not generally increase translational efficiency, since some alleles that strongly suppress 5'-UTL mutations fail to suppress initiation codon mutations. We propose that mitochondrial ribosomes themselves recognize a common feature of mRNA 5'-UTLs which, in conjunction with mRNA-specific translational activation, is required for organellar translation initiation.
authors.affiliation: Section of Genetics and Development, Cornell University, Ithaca, New York 14853-2703, USA.
authors.forename: N S
authors.initials: NS
authors.lastname: Green-Willms
authors.forename: T D
authors.initials: TD
authors.lastname: Fox
authors.forename: M C
authors.initials: MC
authors.lastname: Costanzo
mesh_terms: D000483:Alleles; D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D051546:Cyclooxygenase 2; D003576:Electron Transport Complex IV / Q000235:genetics / Q000378:metabolism; D007527:Isoenzymes / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D008928:Mitochondria / Q000235:genetics*; D008969:Molecular Sequence Data; D017354:Point Mutation; D011451:Prostaglandin-Endoperoxide Synthases / Q000235:genetics / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000235:genetics* / Q000378:metabolism; D000077278:RNA, Mitochondrial; D012269:Ribosomal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D012270:Ribosomes / Q000235:genetics* / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics*; D029701:Saccharomyces cerevisiae Proteins; D016415:Sequence Alignment; D013489:Suppression, Genetic
chemical_list: D007527:Isoenzymes; C112000:MRP21 protein, S cerevisiae; C112002:MRP51 protein, S cerevisiae; D008565:Membrane Proteins; D012333:RNA, Messenger; D000077278:RNA, Mitochondrial; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; C029305:mitochondrial messenger RNA; C032643:ribosomal protein S21; D051546:Cyclooxygenase 2; D011451:Prostaglandin-Endoperoxide Synthases; C093750:COX3 protein, S cerevisiae; D003576:Electron Transport Complex IV