Abstract |
A 4333-bp novel human cDNA sequence designated HEP-COP was isolated from the Hep3B hepatocellular carcinoma cell line by the RACE technique. Within HEP-COP was identified an ORF of 3672 bp encoding a deduced 1224-amino-acid (aa) sequence which exhibited striking homology with the 1201-aa sequence of RET1P, the alpha-subunit of the coatomer complex ( alpha-COP) in Saccharomyces cerevisiae which participates in membrane transport between the endoplasmic reticulum and Golgi apparatus. The aa homology was highest in their N-terminal regions which each contained six WD-40 repeat motifs [Van der Voorn and Ploegh, FEBS Lett. 307 (1992) 131-134], and both proteins were predicted to be hydrophilic with similar estimated molecular masses of 138 324 and 135 599 Da, respectively. Northern blot hybridization demonstrated that HEP-COP was expressed in a wide range of human adult and fetal tissues. RT-PCR analysis revealed no differential expression of HEP-COP in 14 human cancer cell lines, as compared with normal control cells. Considering the close similarities between HEP-COP and yeast alpha-COP, and the ubiquitous expression of HEP-COP implying an essential cellular role, it is likely that HEP-COP is the human homologue of alpha-COP.
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Authors | V T Chow, H H Quek |
Journal | Gene
(Gene)
Vol. 169
Issue 2
Pg. 223-7
(Mar 09 1996)
ISSN: 0378-1119 [Print] Netherlands |
PMID | 8647451
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Coatomer Protein
- DNA, Complementary
- Membrane Proteins
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Topics |
- Amino Acid Sequence
- Base Sequence
- Blotting, Northern
- Coatomer Protein
- DNA, Complementary
- Genome, Human
- Humans
- Membrane Proteins
(chemistry, genetics)
- Molecular Sequence Data
- Polymerase Chain Reaction
- Sequence Homology, Nucleic Acid
- Tumor Cells, Cultured
- Yeasts
(genetics)
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