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
Biochimiejournal_title
Biochimieauthors
Bermúdez-Cruz RM,García-Mena J,Montañez Cdoi
10.1016/s0300-9084(02)01385-8keywords:
subject
Has Abstractpub_date
2002-04-01 00:00:00pages
321-8issue
4eissn
0300-9084issn
1638-6183pii
S0300908402013858journal_volume
84pub_type
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