Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency
Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important role in recycling proline in various cells and tissues. By using human prolidase cDNA as a probe, a chromosomal gene related to prolidase was isolated from human gene librarie...
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Published in | The Journal of biological chemistry Vol. 265; no. 19; pp. 11306 - 11311 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
05.07.1990
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Subjects | |
Online Access | Get full text |
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Summary: | Prolidase (peptidase D) catalyzes hydrolysis of the di- and tripeptide with carboxyl-terminal proline and plays an important
role in recycling proline in various cells and tissues. By using human prolidase cDNA as a probe, a chromosomal gene related
to prolidase was isolated from human gene libraries. The human prolidase gene is over 130 kilobases long and is split into
15 exons. All of the splice donor and acceptor sites conform to the GT/AG rule. The transcription initiation site was determined
by nuclease S1 mapping and primer extension and was located 131 bases upstream from the initiation codon. A "CAAT" box-like
sequence was present 67 bases upstream from the cap site, but there was no "TATA" box-like sequence. There were seven sets
of sequences resembling the transcription factor Sp1 binding sites. Four were upstream from the cap site, and three were downstream.
We also analyzed findings in patients with prolidase deficiency with respect to major gene re-arrangement. Several hundred
base deletions, including the 14th exon, were identified. Knowledge of the gene structure of human prolidase will facilitate
further studies on the expression and regulation of this gene and provide necessary information for analyses of mutations
in patients with this deficiency. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)38592-8 |