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| PURIFICATION OF COMPONENT-A OF RAB GERANYLGERANYL TRANSFERASE - POSSIBLE IDENTITY WITH THE CHOROIDEREMIA GENE-PRODUCT |
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| Author(s): SEABRA MC, BROWN MS, SLAUGHTER CA, SUDHOF TC, GOLDSTEIN JL |
| Source: CELL Volume: 70 Issue: 6 Pages: 1049-1057 Published: SEP 18 1992 |
| Times Cited: 190 References: 34 |
| Abstract: Rab geranylgeranyl transferase (GG transferase) from rat brain contains two components, A and B. Component B comprises polypeptides of 60 and 38 kd. Here we report the purification of component A, a single 95 kd polypeptide. The holoenzyme attaches H-3-geranyl-geranyl to cysteines in two GTP-binding proteins, Rab3A and Rab1A. The reaction is abolished when both cysteines in the COOH-terminal CysCys sequence of Rab1A are mutated to serines. The mutant protein inhibits transfer of H-3-geranylgeranyl to wild-type Rab1A and Rab3A, suggesting that the enzyme recognizes conserved sequences distinct from the COOH-terminus. Six peptides from rat component A show striking similarity to the product of the defective gene in choroideremia, an X-linked retinal degeneration disease. The choroideremia protein resembles Rab3A GDI, which binds Rab3A. We hypothesize that component A binds conserved sequences in Rab and that component B transfers geranylgeranyl. A defect in this reaction may cause choroideremia. |
| Document Type: Article |
| Language: English |
| Reprint Address: SEABRA, MC (reprint author), UNIV TEXAS, SW MED CTR, DEPT MOLEC GENET, DALLAS, TX 75235 USA |
Addresses:
1. UNIV TEXAS, SW MED CTR, DEPT BIOCHEM, DALLAS, TX 75235 USA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: JN781 |
| ISSN: 0092-8674 |
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