Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease.

Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Research Abstract Details 

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Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Abstract Text:

A Tsuji,C Hine,Y Tamai,K Yonemoto,K Mori,S Yoshida,M Bando,E Sakai,K Mori,T Akamatsu,Y Matsuda,

PACE4 (paired basic amino acid cleaving enzyme) is a member of a family of the mammalian kexin-like proprotein convertases containing a subtilisin-like catalytic domain. Previously we reported seven isoform mRNAs of PACE4 that vary in size and 3'-coding sequence [A. Tsuji et al. (1994) Biochem. Biophys. Res. Commun. 200, 943-950; K. Mori et al. (1997) J. Biochem. 121, 941-948]. To determine the origin of these isoforms, the entire human PACE4 gene has been isolated as a set of overlapping genomic DNA fragments, and analyzed by restriction enzyme digestion and nucleotide sequence determination. The human PACE4 gene spans at least 250 kb and is distributed over 25 exons that range in size from 39 to 1,422 base pairs. Human PACE4 gene is the largest kexin-like proprotein convertase gene reported to date. The most striking feature of its genomic structure is the size of the introns and the number of exons, although the general organization of signal peptide, propeptide, and catalytic domains, which are conserved in this family, is very similar to that reported for other kexin-like protease genes. The structural analysis of PACE4 genomic DNA indicates that multiple PACE4 transcripts are produced as a consequence of alternative RNA splicing events, including exon skipping, and differences in the usage of the inner 5'-splicing donor and polyadenylation sites. A major transcriptional start site was detected 314 bp upstream from the ATG translational start site by primer extension analysis. Sequence analysis of the 5'-flanking region revealed that PACE4 gene lacks TATA and CCAAT boxes in the proximal upstream region of the start site, although potential binding sites for several transcription factors including SP1, AP1, AP2, PEA3, Ets-1, GHF (growth hormone factor)-1, CREB (cyclic AMP response element binding protein), and basic helix-loop-helix proteins, were present. An unusual sequence of six tandem repeats of a nonadecamer (GGCCTGGGGGTTCACCTGC) containing an E box is found in the 5'-flanking region. These results suggest that PACE4 is not a constitutive gene product and its expression is regulated by various transcription factors.

Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Publishing Authors By Initials

A Tsuji,C Hine,Y Tamai,K Yonemoto,K Mori,S Yoshida,M Bando,E Sakai,K Mori,T Akamatsu,Y Matsuda,

For similar genetic processes: gene expression: transcription, genetic research abstracts see: genetic processes: gene expression: transcription, genetic research

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Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 122

Page Numbers: 438-52

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Aug

YEAR: 1997

Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Keywords Mesh Terms:

KEYWORDS: Transcription, Genetic

MESH TERMS: genetics

Chemical & Substance for Abstract: Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease. Information

Substance Name: KEX2 protein, S cerevisiae

Registry Number: EC 3.4.21.61

Grant and Affiliation Information for Genomic organization and alternative splicing of human PACE4 (SPC4), kexin-like processing endoprotease.

AFFILIATION: Department of Biological Science and Technology, Faculty of Engineering, University of Tokushima, Minamijosanjima.

Country: JAPAN

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MEDLINETA: J Biochem

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ACCESSION NUMBER: AB001914

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