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- 1. T-B-NK+ SCID：病因および遺伝学 t b nk scid pathogenesis and genetics
- 2. ミトコンドリアミオパシー：臨床的特徴および診断 mitochondrial myopathies clinical features and diagnosis
- 3. 分子遺伝学の原理 principles of molecular genetics
- 4. 成人における皮膚筋炎および多発性筋炎の臨床症状 clinical manifestations of dermatomyositis and polymyositis in adults
- 5. 炎症性ミオパチーの病因 pathogenesis of inflammatory myopathies
English Journal
- Identification and expression pattern of two novel alternative splicing variants of EEF1D gene of dairy cattle.
- Xie Y1, Yang S1, Cui X1, Jiang L1, Zhang S1, Zhang Q1, Zhang Y1, Sun D2.Author information 1College of Animal Science and Technology, China Agricultural University, Beijing 100193, China; Key Laboratory of Animal Genetics and Breeding of Ministry of Agriculture, National Engineering Laboratory of Animal Breeding, China Agricultural University, Beijing 100193, China.2College of Animal Science and Technology, China Agricultural University, Beijing 100193, China; Key Laboratory of Animal Genetics and Breeding of Ministry of Agriculture, National Engineering Laboratory of Animal Breeding, China Agricultural University, Beijing 100193, China. Electronic address: sundx@cau.edu.cn.AbstractOur recent genome-wide association study (GWAS) has identified 105 genome-wide significant SNPs for milk production traits. Of these, one SNP (rs109661298) for milk fat percentage is located within the first intron of the bovine EEF1D gene on BTA14, thus that the EEF1D gene was considered as a novel candidate in dairy cattle. Until now, however, its genomic organization remains undetermined yet and no studies of EEF1D in relation to milk production traits have been reported. To layout the groundwork for the validation of gene function in dairy cattle, we herein investigated its expression pattern in lactating dairy cows. With rapid amplification of 5' cDNA end (5' RACE), two novel alternatively spliced transcript variants of 1202bp and 2195bp were isolated in bovine mammary in lactation, named EEF1Da and EEF1Db (GenBank: KC190039 and KC190038KC190039KC190038). Such two variants contain the different first exon from each other (exon1a vs exon1b: 294bp vs 1287bp) with no overlap and the same remaining 7 exons. Coding sequence similarity between EEF1Da and EEF1Db and three of human EEF1D transcript variants were 85-88%. With semi-quantitative and quantitative real-time RT-PCR, we found that the mRNA level of EEF1Da was similar to the overall EEF1D mRNA and much higher than EEF1Db in the mammary of lactating cows, indicating EEF1Da functions as the dominant transcript variant to encode the EEF1D protein. Tissue expression pattern showed that the mRNA expression of EEF1D and EEF1Da in mammary gland was significantly higher compared with other 7 tissues (P<0.05, P<0.01) with the exception of EEF1D between mammary and lung. Together, our findings present the first report on the alternative splicing of the bovine EEF1D gene and provided basis for further investigation on function validation of EEF1D in dairy cattle.
- Gene.Gene.2014 Jan 25;534(2):189-96. doi: 10.1016/j.gene.2013.10.061. Epub 2013 Nov 14.
- Our recent genome-wide association study (GWAS) has identified 105 genome-wide significant SNPs for milk production traits. Of these, one SNP (rs109661298) for milk fat percentage is located within the first intron of the bovine EEF1D gene on BTA14, thus that the EEF1D gene was considered as a novel
- PMID 24239553
- Aprataxin resolves adenylated RNA-DNA junctions to maintain genome integrity.
- Tumbale P1, Williams JS2, Schellenberg MJ1, Kunkel TA3, Williams RS4.Author information 11] Laboratory of Structural Biology, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA [2].21] Laboratory of Structural Biology, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA [2] Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA [3].31] Laboratory of Structural Biology, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA [2] Laboratory of Molecular Genetics, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA.4Laboratory of Structural Biology, National Institute of Environmental Health Sciences, NIH, DHHS, Research Triangle Park, North Carolina 27709, USA.AbstractFaithful maintenance and propagation of eukaryotic genomes is ensured by three-step DNA ligation reactions used by ATP-dependent DNA ligases. Paradoxically, when DNA ligases encounter nicked DNA structures with abnormal DNA termini, DNA ligase catalytic activity can generate and/or exacerbate DNA damage through abortive ligation that produces chemically adducted, toxic 5'-adenylated (5'-AMP) DNA lesions. Aprataxin (APTX) reverses DNA adenylation but the context for deadenylation repair is unclear. Here we examine the importance of APTX to RNase-H2-dependent excision repair (RER) of a lesion that is very frequently introduced into DNA, a ribonucleotide. We show that ligases generate adenylated 5' ends containing a ribose characteristic of RNase H2 incision. APTX efficiently repairs adenylated RNA-DNA, and acting in an RNA-DNA damage response (RDDR), promotes cellular survival and prevents S-phase checkpoint activation in budding yeast undergoing RER. Structure-function studies of human APTX-RNA-DNA-AMP-Zn complexes define a mechanism for detecting and reversing adenylation at RNA-DNA junctions. This involves A-form RNA binding, proper protein folding and conformational changes, all of which are affected by heritable APTX mutations in ataxia with oculomotor apraxia 1. Together, these results indicate that accumulation of adenylated RNA-DNA may contribute to neurological disease.
- Nature.Nature.2013 Dec 22. doi: 10.1038/nature12824. [Epub ahead of print]
- Faithful maintenance and propagation of eukaryotic genomes is ensured by three-step DNA ligation reactions used by ATP-dependent DNA ligases. Paradoxically, when DNA ligases encounter nicked DNA structures with abnormal DNA termini, DNA ligase catalytic activity can generate and/or exacerbate DNA da
- PMID 24362567
- Proofreading of noncognate acyl adenylates by an acyl-coenzyme a ligase.
- Manandhar M1, Cronan JE2.Author information 1Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.2Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA; Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA. Electronic address: j-cronan@life.uiuc.edu.AbstractAminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its CoA ester. The noncognate BioW substrate glutaric acid results in hydrolysis of ATP to AMP with formation of only trace amounts of glutaryl-CoA, thereby mimicking pretransfer editing of incorrect aminoacyl-adenylates by aminoacyl-tRNA synthetases.
- Chemistry & biology.Chem Biol.2013 Dec 19;20(12):1441-6. doi: 10.1016/j.chembiol.2013.10.010. Epub 2013 Nov 21.
- Aminoacyl-tRNA synthetases remove (proofread) incorrect substrates and thereby prevent errors in protein synthesis. We report enzyme-catalyzed pretransfer editing by pimeloyl-coenzyme A (CoA) ligase (BioW), a biotin synthetic enzyme that converts pimelate, a seven-carbon dicarboxylic acid, to its Co
- PMID 24269150
Japanese Journal
- The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94Å resolution reveals a possible open form with a wider active-site cleft
- Gao Yong-Gui,Yao Min,Okada Ayuko,Tanaka Isao
- Acta Crystallographica Section F Structural Biology and Crystallization Communications 62(12), 1196-1200, 2006-12-01
- … Bacterial and archaeal 2'-5' RNA ligases, members of the 2H phosphoesterase superfamily, catalyze the linkage of the 5' and 3' exons via a 2'-5'-phosphodiester bond during tRNA-precursor splicing. … The crystal structure of the 2'-5' RNA ligase PH0099 from Pyrococcus horikoshii OT3 was solved at 1.94 Å … Structural comparison with the 2'-5' RNA ligase from Thermus thermophilus HB8 also revealed differences in the RNA precursor-binding region. …
- NAID 120000964876
- Structure-function analysis of the kinase-CPD domain of yeast tRNA ligase (Trl1) and requirements for complementation of tRNA splicing by a plant Trl1 homolog
- WANG LK
- Nucleic Acids Res 34, 517-527, 2006
- NAID 30018413220
- 1S06 超好熱始原菌由来の耐熱性酵素における分子認識
- 今中 忠行,跡見 晴幸,高木 昌宏,藤原 伸介
- 日本生物工学会大会講演要旨集 平成13年度, 10, 2001-08-24
- NAID 110002922644
Related Links
- In enzymology, an asparagine-tRNA ligase (EC 6.1.1.22) is an enzyme that catalyzes the chemical reaction ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn The 3 substrates of this enzyme are ATP, L ...
- The European Bioinformatics Institute ... Synonyms are alternative words or phrases closely related in meaning to the term name, with indication of the relationship between the name and synonym given by the synonym scope.
Related Pictures
★リンクテーブル★
| リンク元 | 「tRNAリガーゼ」「RNA ligase」 |
| 拡張検索 | 「tryptophan-tRNA ligase」「aspartate-tRNA ligase」「cysteine-tRNA ligase」「tyrosine-tRNA ligase」 |
| 関連記事 | 「tRNA」「ligase」「tRNAs」 |
「tRNAリガーゼ」
- 英
- tRNA ligase
- 関
- RNAリガーゼ
「RNA ligase」
「tryptophan-tRNA ligase」
「aspartate-tRNA ligase」
「cysteine-tRNA ligase」
「tyrosine-tRNA ligase」
「tRNA」
[★] トランスファーRNA, transfer RNA, 転位RNA