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MOD5 Mod5p

MOD5, Mod5p, tRNA isopentenyltransferase, IPTase
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Top mentioned proteins: CIs, CAN, STEP, ACID, V1a
Papers on MOD5
Defective i6A37 modification of mitochondrial and cytosolic tRNAs results from pathogenic mutations in TRIT1 and its substrate tRNA.
Taylor et al., Newcastle upon Tyne, United Kingdom. In Plos Genet, 2014
Using next-generation exome sequencing, we identified in a patient with severe combined mitochondrial respiratory chain defects and corresponding perturbation in mitochondrial protein synthesis, a homozygous p.Arg323Gln mutation in TRIT1.
Overexpression of the cytosolic cytokinin oxidase/dehydrogenase (CKX7) from Arabidopsis causes specific changes in root growth and xylem differentiation.
Werner et al., Berlin, Germany. In Plant J, 2014
Interestingly, enhanced protoxylem formation together with reduced primary root growth was also found in the cZ-deficient tRNA isopentenyltransferase mutant ipt2,9.
The MiaA tRNA modification enzyme is necessary for robust RpoS expression in Escherichia coli.
Gottesman et al., Washington, D.C., United States. In J Bacteriol, 2014
We screened mutants of several RNA modification enzymes for an effect on RpoS expression and identified the miaA gene, encoding a tRNA isopentenyltransferase, as necessary for full expression of both an rpoS750-lacZ translational fusion and the RpoS protein.
Human cells have a limited set of tRNA anticodon loop substrates of the tRNA isopentenyltransferase TRIT1 tumor suppressor.
Maraia et al., Bethesda, United States. In Mol Cell Biol, 2013
Human TRIT1 is a tRNA isopentenyltransferase (IPTase) homologue of Escherichia coli MiaA, Saccharomyces cerevisiae Mod5, Schizosaccharomyces pombe Tit1, and Caenorhabditis elegans GRO-1 that adds isopentenyl groups to adenosine 37 (i6A37) of substrate tRNAs.
Identification of two additional members of the tRNA isopentenyltransferase family in Physcomitrella patens.
Nicander et al., Uppsala, Sweden. In Plant Mol Biol, 2013
The cloned genes were able to functionally complement a yeast mutant lacking tRNA isopentenyltransferase.
Expanding the yeast prion world: Active prion conversion of non-glutamine/asparagine-rich Mod5 for cell survival.
Tanaka et al., Wako, Japan. In Prion, 2013
In order to fill this gap, we searched for novel yeast prion proteins lacking Gln/Asn-rich domains via a genome-wide screen based on cross-seeding between two heterologous proteins and identified Mod5, a yeast tRNA isopentenyltransferase, as a novel non-Gln/Asn-rich yeast prion protein.
A yeast prion, Mod5, promotes acquired drug resistance and cell survival under environmental stress.
Impact
GeneRIF
Tanaka et al., Wako, Japan. In Science, 2012
identified Mod5 as a yeast prion protein and found that its prion conversion in yeast regulated the sterol biosynthetic pathway for acquired cellular resistance against antifungal agents; selective pressure by antifungal drugs on yeast facilitated the de novo appearance of Mod5 prion states for cell survival
Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases.
GeneRIF
Maraia et al., Bethesda, United States. In Rna, 2011
show that Tit1p accommodates a broader range of substrates than Mod5p
Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation.
Sessa et al., New Haven, United States. In Embo J, 2011
Dol-P is synthesized by the successive condensation of isopentenyl diphosphate (IPP), with farnesyl diphosphate catalysed by a cis-isoprenyltransferase (cis-IPTase) activity.
A catalytic role for Mod5 in the formation of the Tea1 cell polarity landmark.
GeneRIF
Sawin et al., Edinburgh, United Kingdom. In Curr Biol, 2010
Data suggest that rather than acting simply as a Tea1 receptor or as a molecular "glue" to retain Tea1, Mod5 functions catalytically to stimulate incorporation of Tea1 into a stable tip-associated cluster network.
Snapshots of dynamics in synthesizing N(6)-isopentenyladenosine at the tRNA anticodon.
Tanaka et al., Sapporo, Japan. In Biochemistry, 2009
We have determined a series of crystal structures of bacterial tRNA isopentenyltransferase (MiaA) in apo- and tRNA-bound forms, which completely render snapshots of substrate selections during the modification of RNA.
Ethnic differences in frequencies of gene polymorphisms in the MYCL1 region and modulation of lung cancer patients' survival.
GeneRIF
Dragani et al., Milano, Italy. In Lung Cancer, 2007
The rare allele of TRIT1 Phe202Leu SNP was approximately seven-fold more frequent in Asian than in Caucasian subjects and three additional SNPs in the TRIT1 gene showed ethnic differences in allelic frequencies
Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.
ZoĊ‚adek et al., Warsaw, Poland. In Acta Biochim Pol, 2004
Dimethylallyl diphosphate, an isomer of isopentenyl diphosphate, is a common substrate of Mod5p, a tRNA modifying enzyme, and the farnesyl diphosphate synthase Erg20p, the key enzyme of the isoprenoid pathway.
Distinct isoprenoid origins of cis- and trans-zeatin biosyntheses in Arabidopsis.
Sakakibara et al., Japan. In J Biol Chem, 2004
On the other hand, AtIPT2, a tRNA isopentenyltransferase, was detected in the cytosol.
Identification and characterization of a cDNA encoding a long-chain cis-isoprenyltranferase involved in dolichyl monophosphate biosynthesis in the ER of brain cells.
Waechter et al., Lexington, United States. In Biochem Biophys Res Commun, 2004
A long-chain cis-isoprenyltransferase (cis-IPTase) located in the endoplasmic reticulum (ER) catalyzes the chain elongation stage in the pathway for the de novo biosynthesis of dolichyl monophosphate (Dol-P) in eukaryotic cells.
How single genes provide tRNA processing enzymes to mitochondria, nuclei and the cytosol.
Review
Hopper et al., Louisville, United States. In Biochimie, 1993
TRM1, MOD5 and CCA1 are yeast genes that provide tRNA processing enzymes to mitochondria and the nuclear/cytosolic compartments.
Antisuppression of class I suppressors in an isopentenylated-transfer RNA deficient mutant of Saccharomyces cerevisiae.
Laten, Chicago, United States. In Curr Genet, 1984
As expected, the antisuppressor mutation, mod5-1, restricted the capacity of all eight tyrosine-inserting ochre suppressors to suppress nonsense mutations.
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