Inorganic phosphate, arsenate, and vanadate enhance exonuclease transcript cleavage by RNA polymerase by 2000-fold

Proceedings of the National Academy of Sciences of the United States of America
Max E Gottesman, Arkady Mustaev

Abstract

Inorganic Pi is involved in all major biochemical pathways. Here we describe a previously unreported activity of Pi We show that Pi and its structural mimics, vanadate and arsenate, enhance nascent transcript cleavage by RNA polymerase (RNAP). They engage an Mg2+ ion in catalysis and activate an attacking water molecule. Pi, vanadate, and arsenate stimulate the intrinsic exonuclease activity of the enzyme nearly 2,000-fold at saturating concentrations of the reactant anions and Mg2+ This enhancement is comparable to that of specialized transcript cleavage protein factors Gre and TFIIS (3,000- to 4,000-fold). Unlike these protein factors, Pi and its analogs do not stimulate endonuclease transcript cleavage. Conversely, the protein factors only marginally enhance exonucleolytic cleavage. Pi thus complements cellular protein factors in assisting hydrolytic RNA cleavage by extending the repertoire of RNAP transcript degradation modes.

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Citations

May 1, 2020·Physiological Reviews·Nati HernandoEleanor Lederer
Oct 24, 2018·Biological Trace Element Research·Samuel TreviñoEnrique González-Vergara
Nov 2, 2019·Transcription·Max E Gottesman, Arkady Mustaev
May 28, 2019·Frontiers in Microbiology·Andrea FirrincieliMartina Cappelletti

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