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The First Poly(A) Polymerase from Alphaproteobacteria.

Igor P Oscorbin1,2, Maria S Kunova1,2, Maxim L Filipenko1

  • 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences (ICBFM SB RAS), 8, Lavrentiev Avenue, Novosibirsk 630090, Russia.

International Journal of Molecular Sciences
|March 14, 2026
PubMed
Summary

Researchers characterized the first bacterial poly(A) polymerase (PAP) from Alphaproteobacteria, Marinobacter lipolyticus (Mli PAP). This study reveals Mli PAP

Keywords:
Marinobacter lipolyticusPAPpcnBpolyA-polymerasepolyadenylation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Bacterial poly(A) polymerases (PAPs) are crucial for RNA metabolism.
  • PAPs are poorly understood outside Gammaproteobacteria.

Purpose of the Study:

  • To clone and biochemically characterize the first bacterial poly(A) polymerase (PAP) from the Alphaproteobacteria class, specifically from Marinobacter lipolyticus (Mli PAP).
  • To investigate the enzymatic properties and substrate preferences of Mli PAP.
  • To compare Mli PAP with its counterparts in other bacterial classes.

Main Methods:

  • Homology-based screening using E. coli PAP-1 to identify Mli PAP.
  • Expression of Mli PAP in E. coli and purification as a DsbA fusion protein.
  • Biochemical assays to determine optimal activity, substrate preference, cofactor requirements, and salt dependency.

Main Results:

  • Mli PAP shares 54.8% sequence identity with E. coli PAP-1.
  • Optimal activity at 30°C with Mg2+ as the preferred cofactor.
  • ATP is the preferred substrate, with a K m comparable to E. coli PAP-1.
  • Mli PAP exhibits salt-dependent activity, with optimal polyadenylation in KCl, contrasting with its host's halophilic nature.

Conclusions:

  • This study presents the first functional characterization of a PAP from Alphaproteobacteria.
  • The findings expand the understanding of PAP diversity and biochemical properties.
  • Mli PAP's unique salt-dependent activity suggests potential biotechnological applications.