PMID: 7033963Jan 1, 1982Paper

Direct photoaffinity labeling of an allosteric site on subunit protein M1 of mouse ribonucleotide reductase by dTTP

Proceedings of the National Academy of Sciences of the United States of America
S ErikssonD W Martin

Abstract

The protein M1 subunit of ribonucleotide reductase contains at least two allosteric nucleotide binding sites that control the capacity of the enzyme to reduce ribonucleotides to the deoxyribonucleotides required for DNA synthesis. Direct photoaffinity labeling of partially purified protein M1 from mouse T-lymphoma (S49) cells was observed after UV irradiation in the presence of dTTP at 0 degrees C. The relative molar incorporation of nucleotide per subunit was 4-8%. Competition experiments showed that the dTTP was bound to an allosteric domain genetically and kinetically defined as the substrate specificity site of the enzyme. An altered protein M1 isolated from a thymidine-resistant mutant cell line showed significantly decreased photoincorporation of dTTP, consistent with the fact that its CDP reductase activity is resistant to feedback inhibition by dTTP. Specific photolabeling of several other proteins with pyrimidine and purine nucleotides was also found, indicating the general usefulness of direct photoaffinity labeling in the study of enzymes involved in nucleotide and nucleic acid metabolism.

References

Jul 10, 1979·Biochemistry·Y EngströmM Akerman
Jan 1, 1979·Annual Review of Biochemistry·L Thelander, P Reichard

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Citations

Jan 1, 1984·Advances in Enzyme Regulation·F MaleyG Maley
Jan 1, 1984·Pharmacology & Therapeutics·L M Nutter, Y C Cheng
Aug 1, 1984·The Journal of Cell Biology·W A BraellJ E Rothman
Feb 3, 2005·Molecular Microbiology·Michael W WhiteBoris Striepen
May 15, 1984·Archives of Biochemistry and Biophysics·R G Hards, J A Wright

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