Polynucleotide phosphorylase binds to ssRNA with same affinity as to ssDNA.

Abstract:

:Polynucleotide phosphorylase (PNPase, polyribonucleotide nucleotidyltransferase, EC 2.7.7.8) is a multifunctional protein, with a 3'-5' processive exoribonuclease, a Pi exchange, an RNA polymerase and an autoregulatory activity. The interaction between this enzyme and the mRNA target is crucial for its activities. In the present study, we characterized the interaction of PNPase with its mRNA regulatory region and ssRNA, as well as with ssDNA and dsDNA by determining K(d). Our results indicate that PNPase has high affinity for its mRNA, ssRNA and for ssDNA (K(d) approximately 10-20 nM). However, this enzyme exhibits a lower affinity for dsDNA (K(d) approximately 200-1400 nM). Possible implications of these results on the molecular mechanisms by which PNPase is regulated and degrades mRNA are discussed.

journal_name

Biochimie

journal_title

Biochimie

authors

Bermúdez-Cruz RM,García-Mena J,Montañez C

doi

10.1016/s0300-9084(02)01385-8

keywords:

subject

Has Abstract

pub_date

2002-04-01 00:00:00

pages

321-8

issue

4

eissn

0300-9084

issn

1638-6183

pii

S0300908402013858

journal_volume

84

pub_type

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