Posttranslationally modified ornithine decarboxylase may regulate RNA polymerase I activity.

Abstract:

:Purified ornithine decarboxylase (EC 4.1.1.17, ODC) transamidated with four putrescine moieties on four glutamine residues through the action of transglutaminase (EC 2.3.2.13, TGase) purified from guinea pig liver, when added to isolated rat liver nuclei, stoichiometrically increased the activity of RNA polymerase I (EC 2.7.7.6). The increase was relative to the pmoles of purified conjugated ODC added to the reaction and could be reinitiated after the reaction had plateaued by the further addition of ODC-putrescine conjugate. The kinetics of the reaction suggest that the ODC-putrescine conjugate was not reused but degraded after each initiation. Otherwise, the rapid plateau would not be observed. The repeated addition of 278 pmoles of purified ODC-putrescine conjugate to rat liver nuclear preparations containing 200 micrograms total protein consistently stimulated the incorporation of 600-700 pmoles UMP/mg protein. We suggest that ODC transamidated by its product putrescine may be the posttranslationally modified 65,000 Mr protein which has been reported by several laboratories to serve as a labile subunit of RNA polymerase I.

journal_name

Biochem Pharmacol

journal_title

Biochemical pharmacology

authors

Russell DH,Manen CA

doi

10.1016/0006-2952(82)90614-1

subject

Has Abstract

pub_date

1982-11-01 00:00:00

pages

3373-8

issue

21

eissn

0006-2952

issn

1873-2968

pii

0006-2952(82)90614-1

journal_volume

31

pub_type

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