The nuclear protein PH5P of the inter-alpha-inhibitor superfamily: a missing link between poly(ADP-ribose)polymerase and the inter-alpha-inhibitor family and a novel actor of DNA repair?

FEBS Lett. 1999 Mar 5;446(1):6-8. doi: 10.1016/s0014-5793(99)00173-8.

Abstract

Poly(ADP-ribose)polymerase is a nuclear NAD-dependent enzyme and an essential nick sensor involved in cellular processes where nicking and rejoining of DNA strands are required. The inter-alpha-inhibitor family is comprized of several plasma proteins that all harbor one or more so-called heavy chains designated H1-H4. The latter originate from precursor polypeptides H1P-H4P whose upper two thirds are highly homologous. We now describe a novel protein that includes (i) a so-called BRCT domain found in many proteins involved in DNA repair, (ii) an area that is homologous to the NAD-dependent catalytic domain of poly(ADP-ribose)polymerase, (iii) an area that is homologous to the upper two thirds of precursor polypeptides H1P-H4P and (iv) a proline-rich region with a potential nuclear localization signal. This protein now designated PH5P points to as yet unsuspected links between poly(ADP-ribose)polymerase and the inter-alpha-inhibitor family and is likely to be involved in DNA repair.

Publication types

  • Review

MeSH terms

  • Alpha-Globulins / genetics
  • Alpha-Globulins / metabolism*
  • Animals
  • DNA Repair*
  • Humans
  • Nuclear Proteins / metabolism*
  • Poly(ADP-ribose) Polymerases / metabolism*

Substances

  • Alpha-Globulins
  • Nuclear Proteins
  • PARP4 protein, human
  • inter-alpha-inhibitor
  • Poly(ADP-ribose) Polymerases