Abstract:
:Saccharomyces cerevisiae is an ideal host from which to obtain high levels of posttranslationally modified eukaryotic proteins for x-ray crystallography. However, extensive replacement of methionine by selenomethionine for anomalous dispersion phasing has proven intractable in yeast. We report a general method to incorporate selenomethionine into proteins expressed in yeast based on manipulation of the appropriate metabolic pathways. sam1(-) sam2(-) mutants, in which the conversion of methionine to S-adenosylmethionine is blocked, exhibit reduced selenomethionine toxicity compared with wild-type yeast, increased production of protein during growth in selenomethionine, and efficient replacement of methionine by selenomethionine, based on quantitative mass spectrometry and x-ray crystallography. The structure of yeast tryptophanyl-tRNA synthetase was solved to 1.8 A by using multiwavelength anomalous dispersion phasing with protein that was expressed and purified from the sam1(-) sam2(-) strain grown in selenomethionine. Six of eight selenium residues were located in the structure.
journal_name
Proc Natl Acad Sci U S Aauthors
Malkowski MG,Quartley E,Friedman AE,Babulski J,Kon Y,Wolfley J,Said M,Luft JR,Phizicky EM,DeTitta GT,Grayhack EJdoi
10.1073/pnas.0610337104subject
Has Abstractpub_date
2007-04-17 00:00:00pages
6678-83issue
16eissn
0027-8424issn
1091-6490pii
0610337104journal_volume
104pub_type
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