The conserved Lys-95 charged residue cluster is critical for the homodimerization and enzyme activity of human ribonucleotide reductase small subunit M2

Abstract

Background: Human ribonucleotide reductase small subunit M2 exists in a homodimer form. Results: Charge-altering mutations of the interfacial residue Lys-95 in M2 prevent its dimer assembly, which inhibits the enzyme activity by interfering with the large subunit M1 binding and subcellular distribution. Conclusion: The conserved Lys-95 charged residue cluster mediates M2 homodimerization. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.