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2 results on '"Cellitti S"'

1. Efforts toward the direct experimental characterization of enzyme microenvironments: tyrosine100 in dihydrofolate reductase.

Author

Groff D, Thielges MC, Cellitti S, Schultz PG, and Romesberg FE

Subjects
Catalysis, Mutagenesis, Site-Directed, Protein Conformation, Spectroscopy, Fourier Transform Infrared, Static Electricity, Tetrahydrofolate Dehydrogenase genetics, Tyrosine genetics, Tetrahydrofolate Dehydrogenase chemistry, Tyrosine chemistry
Abstract

State secrets: Site-specific deuteration and FTIR studies reveal that Tyr100 in dihydrofolate reductase plays an important role in catalysis, with a strong electrostatic coupling occurring between Tyr100 and the charge that develops in the hydride-transfer transition state (see picture, NADP(+) purple, Tyr100 green). However, relaying correlated motions that facilitate catalysis from distal sites of the protein to the hydride donor may also be involved.

Published
2009
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2. A facile system for encoding unnatural amino acids in mammalian cells.

Author

Chen PR, Groff D, Guo J, Ou W, Cellitti S, Geierstanger BH, and Schultz PG

Subjects
Amino Acids chemistry, Amino Acyl-tRNA Synthetases genetics, Animals, Archaea genetics, CHO Cells, Cell Line, Cricetinae, Cricetulus, Escherichia coli enzymology, Escherichia coli genetics, Humans, Lysine chemistry, Lysine genetics, Lysine metabolism, Protein Biosynthesis, Proteins genetics, Amino Acids biosynthesis, Amino Acids genetics, Amino Acyl-tRNA Synthetases metabolism, Genetic Code, Lysine analogs & derivatives, Proteins chemistry
Abstract

A shuttle system has been developed to genetically encode unnatural amino acids in mammalian cells using aminoacyl-tRNA synthetases (aaRSs) evolved in E. coli. A pyrrolysyl-tRNA synthetase (PylRS) mutant was evolved in E. coli that selectively aminoacylates a cognate nonsense suppressor tRNA with a photocaged lysine derivative. Transfer of this orthogonal tRNA-aaRS pair into mammalian cells made possible the selective incorporation of this unnatural amino acid into proteins.

Published
2009
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