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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2005-12-2
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pubmed:abstractText |
DNase X is the first human DNase protein identified as being homologous with DNase I. In the present study we describe the isolation of several mammalian DNase X cDNAs and the molecular characterization of their coding proteins. A sequence comparison reveals some conserved characteristics: all the mammalian DNase X proteins have an N-terminal signal peptide, a potential N-linked glycosylation site and a C-terminal hydrophobic domain. Human DNase X, ectopically expressed in HeLa S3 cells, is located in the ER (endoplasmic reticulum) and is modified by an N-linked glycosylation at Asn-243. Gene expression analyses show that the high expression level in muscular tissues, a known feature of human DNASE X, is also observed in mouse DNase X. Interestingly, the translation of porcine and bovine DNase X proteins occurs in the absence of an in-frame AUG initiation codon. We show that their mRNAs utilize a conserved CUG triplet for translation initiation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-10194301,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-10710429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-10858283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-11141064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-12050166,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-12673344,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-15189143,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-1986249,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-3277717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-6245089,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-8062835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-8062836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-8541839,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-8570185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-8654957,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/16107205-9620874
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
392
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
511-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16107205-Amino Acid Sequence,
pubmed-meshheading:16107205-Animals,
pubmed-meshheading:16107205-Base Sequence,
pubmed-meshheading:16107205-Cattle,
pubmed-meshheading:16107205-Codon, Initiator,
pubmed-meshheading:16107205-Consensus Sequence,
pubmed-meshheading:16107205-Deoxyribonucleases,
pubmed-meshheading:16107205-Gene Expression Profiling,
pubmed-meshheading:16107205-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:16107205-HeLa Cells,
pubmed-meshheading:16107205-Humans,
pubmed-meshheading:16107205-Mice,
pubmed-meshheading:16107205-Molecular Sequence Data,
pubmed-meshheading:16107205-Peptide Chain Initiation, Translational,
pubmed-meshheading:16107205-Protein Biosynthesis,
pubmed-meshheading:16107205-RNA, Messenger,
pubmed-meshheading:16107205-Sequence Homology, Amino Acid,
pubmed-meshheading:16107205-Swine
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pubmed:year |
2005
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pubmed:articleTitle |
Physical and biochemical properties of mammalian DNase X proteins: non-AUG translation initiation of porcine and bovine mRNAs for DNase X.
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pubmed:affiliation |
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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