RNA-hydrolyzing activity of human serum albumin and its recombinant analogue

Yulia V Gerasimova; Tatyana V Bobik; Natalya A Ponomarenko; Makhmut M Shakirov; Marina A Zenkova; Nikolai V Tamkovich; Tatyana V Popova; Dmitry G Knorre; Tatyana S Godovikova

doi:10.1016/j.bmcl.2009.12.095

RNA-hydrolyzing activity of human serum albumin and its recombinant analogue

Bioorg Med Chem Lett. 2010 Feb 15;20(4):1427-31. doi: 10.1016/j.bmcl.2009.12.095. Epub 2010 Jan 4.

Authors

Yulia V Gerasimova¹, Tatyana V Bobik, Natalya A Ponomarenko, Makhmut M Shakirov, Marina A Zenkova, Nikolai V Tamkovich, Tatyana V Popova, Dmitry G Knorre, Tatyana S Godovikova

Affiliation

¹ Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, Novosibirsk, Russia.

PMID: 20079637
DOI: 10.1016/j.bmcl.2009.12.095

Abstract

The comparative analysis of RNA-hydrolyzing activity of albumin from human serum and albumin expressed in methylotrophic yeast Pichia pastoris has been carried out. The rate of polyribonucleotide phosphodiester bond cleavage in the presence of recombinant albumin has been found to be similar to that of the reaction mediated by the native protein. According to 31P NMR data, RNA hydrolysis follows the mechanism of intermolecular trans-esterification to yield 2',3'-cyclophosphodiester reaction products that are further slowly hydrolyzed to form nucleoside-3'- and nucleoside-2'-phosphates. Analysis of pH dependence suggests an acid-base mechanism of catalysis. The catalytic activity and substrate specificity of albumin in RNA hydrolysis distinguish it from human ribonucleases.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Base Sequence
Humans
Hydrogen-Ion Concentration
Molecular Sequence Data
RNA / chemistry*
RNA / genetics
Serum Albumin / chemistry*
Serum Albumin / genetics

Substances

Serum Albumin
RNA