Protein farnesyltransferase and geranylgeranyltransferase share a common alpha subunit
- M C Seabra 1, Y Reiss , P J Casey , M S Brown , J L Goldstein
- M C Seabra 1, Y Reiss , P J Casey
- 1Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
- 0Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
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View abstract on PubMed
Summary
This summary is machine-generated.Mammalian prenyltransferases, farnesyltransferase and geranylgeranyltransferase, share a common alpha subunit. Different beta subunits dictate distinct protein specificities for these essential enzymes.
Area Of Science
- Molecular Biology
- Enzymology
- Protein Prenylation
Background
- Mammalian farnesyltransferase is crucial for modifying p21ras proteins with a farnesyl group.
- This enzyme complex consists of alpha and beta subunits, with the beta subunit known to bind p21ras.
- The precise subunit composition and shared components of prenyltransferases remain an area of investigation.
Purpose Of The Study
- To investigate the subunit composition of mammalian farnesyltransferase and related prenyltransferases.
- To determine if the alpha subunit of farnesyltransferase is shared with other prenylating enzymes.
- To elucidate the substrate specificities and structural relationships between different prenyltransferases.
Main Methods
- Enzyme purification and characterization using gel filtration and ion exchange chromatography.
- Immunoprecipitation and immunoblotting using antibodies against the alpha subunit of farnesyltransferase.
- Analysis of protein acceptor specificities for farnesyltransferase and geranylgeranyltransferase.
Main Results
- The alpha subunit of farnesyltransferase is shared with another prenyltransferase that geranylgeranylates Ras-related proteins.
- While exhibiting similar molecular weights, these two enzymes can be separated chromatographically.
- Antibodies against the alpha subunit recognized both enzymes, confirming subunit homology.
- Distinct COOH-terminal amino acid preferences (methionine/serine vs. leucine) were observed for farnesyltransferase and geranylgeranyltransferase, respectively.
Conclusions
- Mammalian farnesyltransferase and geranylgeranyltransferase are distinct heterodimeric enzymes.
- Both enzymes share a common alpha subunit but possess different beta subunits.
- This shared subunit architecture allows for diverse protein prenylation pathways.
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