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Biochimica et Biophysica Acta - Molecular Cell Research
Generically Dependent Continuant
RDF description of Npa3/ScGpn1 carboxy-terminal tail is dispensable for cell viability and RNA polymerase II nuclear targeting but critical for microtubule stability and function - http://orbis.uaslp.mx/vivo/individual/scopus4977
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Npa3/ScGpn1 carboxy-terminal tail is dispensable for cell viability and RNA polymerase II nuclear targeting but critical for microtubule stability and function
Genetic deletion of the essential GTPase Gpn1 or replacement of the endogenous gene by partial loss of function mutants in yeast is associated with multiple cellular phenotypes, including in all cases a marked cytoplasmic retention of RNA polymerase II (RNAPII). Global inhibition of RNAPII-mediated transcription due to malfunction of Gpn1 precludes the identification and study of other cellular function(s) for this GTPase. In contrast to the single Gpn protein present in Archaea, eukaryotic Gpn1 possesses an extension of approximately 100 amino acids at the C-terminal end of the GTPase domain. To determine the importance of this C-terminal extension in Saccharomyces cerevisiae Gpn1, we generated yeast strains expressing either C-terminal truncated (gpn1ΔC) or full-length ScGpn1. We found that ScGpn1ΔC was retained in the cell nucleus, an event physiologically relevant as gpn1ΔC cells contained a higher nuclear fraction of the RNAPII CTD phosphatase Rtr1. gpn1ΔC cells displayed an increased size, a delay in mitosis exit, and an increased sensitivity to the microtubule polymerization inhibitor benomyl at the cell proliferation level and two cellular events that depend on microtubule function: RNAPII nuclear targeting and vacuole integrity. These phenotypes were not caused by inhibition of RNAPII, as in gpn1ΔC cells RNAPII nuclear targeting and transcriptional activity were unaffected. These data, combined with our description here of a genetic interaction between GPN1 and BIK1, a microtubule plus-end tracking protein with a mitotic function, strongly suggest that the ScGpn1 C-terminal tail plays a critical role in microtubule dynamics and mitotic progression in an RNAPII-independent manner. © 2016 Elsevier B.V.
amino acid, 65072-01-7; benomyl, 17804-35-2; guanosine triphosphatase, 9059-32-9; nocodazole, 31430-18-9; phosphatase, 9013-05-2; Benomyl; Bik1 protein, S cerevisiae; Microtubule-Associated Proteins; Monomeric GTP-Binding Proteins; Npa3 protein, S cerevisiae; RNA Polymerase II; Rtr1 protein, S cerevisiae; Saccharomyces cerevisiae Proteins; Transcription Factors; Tubulin Modulators
Benomyl; BIK1; GTPase Gpn1; Microtubules; Npa3/ScGpn1 carboxy terminal tail; Saccharomyces cerevisiae amino acid; benomyl; BIK1 protein; guanosine triphosphatase; nocodazole; Npa3 protein; phosphatase; RNA polymerase II; Rpb1 protein; Rpb2 protein; Rpb3 protein; ScGpn1 protein; unclassified drug; benomyl; Bik1 protein, S cerevisiae; microtubule associated protein; monomeric guanine nucleotide binding protein; Npa3 protein, S cerevisiae; RNA polymerase II; Rtr1 protein, S cerevisiae; Saccharomyces cerevisiae protein; transcription factor; tubulin modulator; archaeon; Article; carboxy terminal sequence; cell function; cell nucleus; cell proliferation; cell vacuole; cell viability; gene interaction; microtubule; microtubule assembly; mitosis; nonhuman; nuclear localization signal; phenotypic variation; physiological process; priority journal; protein polymerization; Saccharomyces cerevisiae; yeast cell; gene deletion; gene expression regulation; genetic transcription; genetics; metabolism; microbial viability; microtubule; protein domain; signal transduction; ultrastructure; Benomyl; Cell Nucleus; Gene Expression Regulation, Fungal; Microbial Viability; Microtubule-Associated Proteins; Microtubules; Monomeric GTP-Binding Proteins; Protein Domains; RNA Polymerase II; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Deletion; Signal Transduction; Transcription Factors; Transcription, Genetic; Tubulin Modulators; Vacuoles