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TRNA splicing endonuclease 2 homolog

sen2, TSEN2, Sen2p, HsSen2
This gene encodes one of the subunits of the tRNA splicing endonuclease. This endonuclease catalyzes the first step in RNA splicing which is the removal of introns. Mutations in this gene have been associated with pontocerebellar hypoplasia type 2. A pseudogene has been identified on chromosome 4. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Feb 2009] (from NCBI)
Top mentioned proteins: Sen54, Sen34, HsSen15, WAVE, Exportin-t
Papers on sen2
Pontocerebellar hypoplasia type 2 and TSEN2: review of the literature and two novel mutations.
Kutsche et al., Hamburg, Germany. In Eur J Med Genet, 2013
Seven different subtypes have been reported (PCH1-7) and mutations in three genes, TSEN2, TSEN34 and TSEN54 encoding three of four subunits of the tRNA splicing endonuclease complex have been found to underlie PCH2, PCH4 and PCH5.
Clinical, neuroradiological and genetic findings in pontocerebellar hypoplasia.
Poll-The et al., Amsterdam, Netherlands. In Brain, 2011
Mutations in the transfer RNA splicing endonuclease subunit genes (TSEN54, TSEN2, TSEN34) were found to be associated with pontocerebellar hypoplasia types 2 and 4. Mutations in the mitochondrial transfer RNA arginyl synthetase gene (RARS2) were associated with pontocerebellar hypoplasia type 6.
Pontocerebellar hypoplasia: clinical, pathologic, and genetic studies.
Bertini et al., Genova, Italy. In Neurology, 2010
METHODS: We retrospectively selected a cohort of 12 children from 9 Italian families with MRI of hypoplastic pontocerebellar structures and clinical manifestations suggesting either PCH2 or PCH4 and submitted them to direct sequencing of the genes encoding the 4 subunits of the TSEN complex, namely TSEN54, TSEN34, TSEN15, and TSEN2.
Molecular and neuroimaging findings in pontocerebellar hypoplasia type 2 (PCH2): is prenatal diagnosis possible?
Dobyns et al., Los Angeles, United States. In Am J Med Genet A, 2010
Most patients with PCH2 have mutations in TSEN54, with occasional mutations found in TSEN34 or TSEN2, genes that encode subunits of tRNA splicing endonuclease.
Cytoplasmic splicing of tRNA in Saccharomyces cerevisiae.
Endo et al., Nagoya, Japan. In Genes Cells, 2007
We isolated a new reversible allele of temperature-sensitive (ts) sen2 (HA-sen2-42), which encodes a mutant form of one of the catalytic subunits of yeast splicing endonuclease.
MMASS: an optimized array-based method for assessing CpG island methylation.
Brenton et al., Cambridge, United Kingdom. In Nucleic Acids Res, 2005
Comparison with previous methylation data for HCT116 and validation of CpG islands from PXMP4, SFRP2, DCC, RARB and TSEN2 confirmed the accuracy of MMASS-v2 results.
Cotranscription and intergenic splicing of the PPARG and TSEN2 genes in cattle.
Amarger et al., Limoges, France. In Bmc Genomics, 2005
There is evidence of cotranscription and intergenic splicing events between the PPARG gene and the neighboring gene TSEN2 in cattle. Two types of chimeric transcripts are observed.
[Two cases of gastric cancers with lung metastases responding to weekly administration of paclitaxel].
Mitsuyama et al., Kitakyūshū, Japan. In Gan To Kagaku Ryoho, 2004
Case 2, another 73 year-old man with multiple lung metastases at 7 months after distal gastrectomy for Borrmann 3 type gastric cancer (4 x 3.5 cm, muc, P0 cy(-) H0 sen2, stage III B, ly1, v0) received weekly paclitaxel 110 mg (80 mg/m2).
Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' end formation.
Trotta et al., South Plainfield, United States. In Cell, 2004
This enzyme consists of HsSen2, HsSen34, HsSen15, and HsSen54, homologs of the yeast tRNA endonuclease subunits.
N-domain angiotensin I-converting enzyme with 80 kDa as a possible genetic marker of hypertension.
Casarini et al., São Paulo, Brazil. In Hypertension, 2003
The urine from SHR, SHR-SP, and SHRen presented 80 (S-1, SP-1, Sen-1) and 65 (S-2, SP-2, Sen-2) kDa ACE forms, differing from the urine profile of normotensive rats, but similar to that described for hypertensive patients.
Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing endonuclease mainly localizes on the mitochondria.
Endo et al., Nagoya, Japan. In Mol Biol Cell, 2003
In yeast, the tRNA splicing endonuclease that cleaves the exon-intron junctions of pre-tRNAs consists of Sen54p, Sen2p, Sen34p, and Sen15p and was thought to be an integral membrane protein of the inner nuclear envelope.
The yeast tRNA splicing endonuclease: a tetrameric enzyme with two active site subunits homologous to the archaeal tRNA endonucleases.
Abelson et al., Pasadena, United States. In Cell, 1997
Two subunits, Sen2p and Sen34p, contain a homologous domain of approximately 130 amino acids.
Common senescent cell-specific antibody epitopes on fibronectin in species and cells of varied origin.
Smith et al., Houston, United States. In J Cell Physiol, 1992
We have previously shown that monoclonal antibodies SEN-1, SEN-2, and SEN-3 react to epitopes on fibronectin that are exposed when human diploid fibroblasts become senescent.
Accumulation of pre-tRNA splicing '2/3' intermediates in a Saccharomyces cerevisiae mutant.
Abelson et al., Pasadena, United States. In Embo J, 1990
Surprisingly, the splicing defect does not appreciably affect cell growth at normal or elevated temperatures, but does confer a pseudo cold-sensitive phenotype of retarded growth at 15 degrees C. The mutant falls into the complementation group SEN2 previously defined by the isolation of mutants defective for tRNA splicing in vitro [Winey, M. and Culbertson, M.R. (1988) Genetics, 118, 609-617], although its phenotypes are distinct from those of the previous sen2 isolates.
Mutations affecting the tRNA-splicing endonuclease activity of Saccharomyces cerevisiae.
Culbertson et al., Madison, United States. In Genetics, 1988
The sen2-1 mutation does not confer a detectable growth defect, but causes a temperature-dependent reduction of in vitro endonuclease activity.
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