Rpm2p, a component of yeast mitochondrial RNase P, acts as a transcriptional activator in the nucleus.
Rpm2p, a protein subunit of yeast mitochondrial RNase P, has another function that is essential in cells lacking the wild-type mitochondrial genome. This function does not require the mitochondrial leader sequence and appears to affect transcription of nuclear genes. Rpm2p expressed as a fusion protein with green fluorescent protein localizes to the nucleus and activates transcription from promoters containing lexA-binding sites when fused to a heterologous DNA binding domain, lexA. The transcriptional activation region of Rpm2p contains two leucine zippers that are required for transcriptional activation and are conserved in the distantly related yeast Candida glabrata. The presence of a mitochondrial leader sequence does not prevent a portion of Rpm2p from locating to the nucleus, and several observations suggest that the nuclear location and transcriptional activation ability of Rpm2p are physiologically significant. The ability of RPM2 alleles to suppress tom40-3, a temperature-sensitive mutant of a component of the mitochondrial import apparatus, correlates with their ability to transactivate the reporter genes with lexA-binding sites. In cells lacking mitochondrial DNA, Rpm2p influences the levels of TOM40, TOM6, TOM20, TOM22, and TOM37 mRNAs, which encode components of the mitochondrial import apparatus, but not that of TOM70 mRNA. It also affects HSP60 and HSP10 mRNAs that encode essential mitochondrial chaperones. Rpm2p also increases the level of Tom40p, as well as Hsp60p, but not Atp2p, suggesting that some, but not all, nucleus-encoded mitochondrial components are affected.
Stribinskis
Vilius
V
Department of Biochemistry and Molecular Biology, School of Medicine, University of Louisville, Louisville, KY 40292, USA.
Heyman
Hong-Chen
HC
Ellis
Steven R
SR
Steffen
Marlene C
MC
Martin
Nancy C
NC
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism*; D018834:Chaperonin 60 / Q000378:metabolism; D016350:Leucine Zippers / Q000502:physiology; D026901:Membrane Transport Proteins / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D033681:Mitochondrial Membrane Transport Proteins; D006180:Proton-Translocating ATPases / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D043262:Ribonuclease P / Q000235:genetics / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism; D015534:Trans-Activators / Q000235:genetics / Q000502:physiology*; D014158:Transcription, Genetic / Q000502:physiology; D000099160:LexA Repressor Protein
D001426:Bacterial Proteins; D018834:Chaperonin 60; D026901:Membrane Transport Proteins; D033681:Mitochondrial Membrane Transport Proteins; D006180:Proton-Translocating ATPases; D011993:Recombinant Fusion Proteins; D043262:Ribonuclease P; D029701:Saccharomyces cerevisiae Proteins; D012697:Serine Endopeptidases; D015534:Trans-Activators; D000099160:LexA Repressor Protein; C066555:Tom40 protein, S cerevisiae; C471230:ATP2 protein, S cerevisiae