Document Detail


Molecular probing of the Saccharomyces cerevisiae sterol 24-C methyltransferase reveals multiple amino acid residues involved with C2-transfer activity.
MedLine Citation:
PMID:  18503783     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two families of sterol C24-methyltransferase (SMT) are responsible for the formation of the ergostane (C(1)-transfer activity; SMT1) and stigmastane (C(2)-transfer activity: SMT2) sterol side chains, respectively. The fungal Saccharomyces cerevisiae SMT1 (Erg6p) operates the first C(1)-transfer in concerted fashion to form a single product whereas the protozoan and plant SMTs are bifunctional capable of catalyzing two sequential, mechanistically distinct C-methylation activities in the conversion of a Delta(24)-sterol acceptor to diverse doubly alkylated products. Previous mutation of the amino acids of Erg6p at D79, Y81 and E82 afforded C(1) or C(2)-transfer activities typical of the protozoan and plant SMT. In this study, scanning mutagenesis experiments involving a leucine replacement of 52 amino acids in Erg6p followed by substitution of key residues with functionally or structurally similar amino acids indicated that 5 new residues at positions Y192, G217, G218, T219 and Y223 can switch the course of C(1)-transfer activity to include plant-like C(2)-transfer activity. The data support a model in which several conserved and non-conserved amino acids located in distinct regions of the Erg6p regulate the course of the C-methylation reaction toward product differences.
Authors:
Kulothungan Ganapathy; Christopher W Jones; Camille M Stephens; Rit Vatsyayan; Julie A Marshall; W David Nes
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-05-08
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1781     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:    2008 Jun-Jul
Date Detail:
Created Date:  2008-06-23     Completed Date:  2008-08-15     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  344-51     Citation Subset:  IM    
Affiliation:
Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 79409-1061, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acids / chemistry*
Methyltransferases / chemistry,  genetics,  metabolism*
Molecular Probes*
Molecular Sequence Data
Mutagenesis
Saccharomyces cerevisiae / enzymology*
Sequence Homology, Amino Acid
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Molecular Probes; EC 2.1.1.-/Methyltransferases; EC 2.1.1.41/delta 24-sterol methyltransferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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