共查询到20条相似文献,搜索用时 46 毫秒
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Heath Cole Knight Thomas R. Reynolds Gregory A. Meyers Robert J. Pomponio Gregory A. Buck Barry Wolf 《Mammalian genome》1998,9(4):327-330
Biotinidase cleaves biotin from biocytin, thereby recycling the vitamin. We have determined the structure of the human biotinidase
gene. A genomic clone, containing three exons that code for the mature enzyme, was obtained by screening a human genomic bacteriophage
library with the biotinidase cDNA by plaque hybridization. To obtain a clone containing the most 5′ exon of the biotinidase
cDNA, a human PAC library by PCR was screened. The human biotinidase gene is organized into four exons and spans at least
23 kb. The 5′-flanking region of exon 1 contains a CCAAT element, three initiator sequences, an octamer sequence, three methylation
consensus sites, two GC boxes, and one HNF-5 site, but has no TATA element. The region from nt −600 to +400 has features of
a CpG island and resembles a housekeeping gene promoter. The structure and sequence of this gene are useful for identifying
and characterizing mutations that cause biotinidase deficiency.
Received: 30 September 1997 / Accepted: 5 December 1997 相似文献
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We have identified and characterized the complete cDNA and gene for the mouse MutS homolog 5 (Msh5), as a step toward understanding the molecular genetic mechanisms involved in the biological function of this new MutS homologous
protein in mammals. The Msh5 cDNA contains a 2502-bp open reading frame (ORF) that encodes an 833-amino acid protein with
a predicted molecular weight of 92.6 kDa, which shares 89.8% amino acid sequence identity with the human hMSH5 protein. Northern
blot analysis demonstrated the presence of a Msh5 mRNA approximately 2.9-kb in length, most abundantly expressed in mouse
testis. Yeast two-hybrid analysis indicated that the mouse Msh5 protein positively interacted with the human hMSH4 protein—suggesting
that Msh5 shares common functional properties with its human counterpart. Sequence and structural analyses show that the mouse
gene Msh5 spans approximately 18 kb and contains 24 exons that range in length from 36 bp for exon 7 to 392 bp for exon 1. Structural
comparison with the human hMSH5 gene revealed that all of the Msh5 internal exons, but not introns, are conserved in length with the human hMSH5. The Msh5 gene is located on mouse Chromosome (Chr) 17 in a location that is syntenic to the region of human Chr 6 harboring the hMSH5
gene. The identification and characterization of Msh5 will facilitate studies of the potential functional roles of this new member of the MutS family.
Received: 11 May 1999 / Accepted: 16 July 1999 相似文献
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Yan Shi Xin-Ping Zhu Jing-Kui Yin Qi-Ya Zhang Jian-Fang Gui 《Molecular biology reports》2010,37(3):1483-1493
Interferon-regulatory factor 1 (IRF-1) is the first member of IRF family, which is involved in many biological processes such
as immune response, antiviral defense, cell growth regulation, and apoptosis. In this study, an IRF-1 gene, EcIRF-1, was isolated and characterized from orange-spotted grouper (Epinephelus coioides). The full-length cDNA of EcIRF-1 is 1,730 bp, including an open reading frame of 906 bp, a 5′-terminal untranslated region (5′-UTR) of 153 bp, and a 3′-UTR
of 671 bp. The EcIRF-1 gene consists of 10 exons and 9 introns, spanning over approximate 4.3 kb of genomic sequence. The 5′-UTR sequence contains
an exon and an intron, and the 3′-UTR sequence is included in the last exon. Expression analysis by real-time PCR reveals
that the EcIRF-1 gene is ubiquitously expressed in various healthy fish tissues, whereas its expression is upregulated in vivo in response
to polyinosinic–polycytidylic acid or lipopolysaccharide stimulation. Subcellular localization analysis shows the EcIRF-1 is an intranuclearly localized and immobile protein in the cultured fish cells. Data presented in this paper provide
an important base to further understand EcIRF-1 gene function and its regulation associated with interferon immune system in orange-spotted grouper. 相似文献
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Euphemia Leung Randal W. Berg Ries Langley John Greene Lisa A. Raymond Meena Augustus Jian Ni Kenneth C. Carter Nigel Spurr K. H. Andy Choo G. W. Krissansen 《Immunogenetics》1997,46(2):111-119
MAdCAM-1, the endothelial addressin cell adhesion molecule-1, interacts preferentially with the leukocyte β7 integrin LPAM-1
(α4β7), but also with L-selectin, and with VLA-4 (α4β1) on myeloid cells, and serves to direct leukocytes into mucosal and
inflamed tissues. Overlapping cosmid and phage λ genomic clones were isolated, revealing that the human MAdCAM-1 gene contains five exons where the signal peptide, two Ig domains, and mucin domain are each encoded by separate exons. The
transmembrane domain, cytoplasmic domain, and 3′ untranslated region are encoded together on exon 5. The mucin domain contains
eight repeats in total that are subject to alternative splicing. Despite the absence of a human counterpart of the third IgA-homologous
domain and lack of sequence conservation of the mucin domain, the genomic organizations of the human and mouse MAdCAM-1 genes are similar. An alternatively spliced MAdCAM-1 variant was identified that lacks exon 4 encoding the mucin domain,
and may mediate leukocyte adhesion to LPAM-1 without adhesion to the alternate receptor, L-selectin. The MAdCAM-1 gene was located at p13.3 on chromosome 19, in close proximity to the ICAM-1 and ICAM-3 genes (p13.2-p13.3). PMA-inducible promotor activity was contained in a 700 base pair 5’ flanking fragment conserved with
the mouse MAdCAM-1 gene including tandem NF-kB sites, and an Sp1 site; and in addition multiple potential AP2, Adh1 (ETF), PEA3, and Sp1 sites.
In summary, the data establish that the previously reported human MAdCAM-1 cDNA does indeed encode the human homologue of mouse MAdCAM-1, despite gross dissimilarities in the MAdCAM-1 C-terminal structures.
Received: 5 December 1996 / Revised: 2 January 1997 相似文献