Dramatic increase in poly(A) synthesis after infection of Molt-3 cells with HIV.

Abstract

Infection of Molt-3 cells with human immunodeficiency virus-1 (HIV-1) was found to cause a rapid increase in extractable poly(A) polymerase activity, while the activity of poly(A) degrading endoribonuclease IV strongly decreased at the same time. The increase in poly(A) polymerase activity seems not to be due to a change in the actual number of enzyme molecules, but rather to posttranslational enzyme modification, most likely caused by phosphorylation by nuclear protein kinase NI or protein kinase C. Both kinases were found to be able to phosphorylate poly(A) polymerase in vitro [homogeneous enzyme as well as poly(A) polymerase in intact nuclei]. Phosphoamino acid analysis revealed an incorporation of phosphate into serine and, to a lower extent, into threonine residues of the enzyme protein; no phosphotyrosine could be detected. In the nucleus, the poly(A) polymerase and the endoribonuclease IV are bound to the nuclear matrix. The phosphorylation related enhancement of nuclear poly(A) polymerase activity could be abolished by addition of the zinc and copper chelator o-phenanthroline, which inhibited zinc-containing purified poly(A) polymerase and destroyed the poly(A) polymerase containing nuclear matrix structure, resulting in a solubilization of the enzyme.

• Authors: H C Schröder, M Rottmann, R Wenger, W E Müller
• Journal: Virus research (Virus Res) Vol. 15 Issue 3 Pg. 251-66 (Mar 1990) ISSN: 0168-1702 [Print] Netherlands
• PMID: 2343676 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Poly A
• Polynucleotide Adenylyltransferase
• Endoribonucleases
• endoribonuclease IV
• Zinc

Topics

• Cell Line
• Endoribonucleases (metabolism)
• HIV-1 (metabolism)
• Phosphorylation
• Poly A (biosynthesis)
• Polynucleotide Adenylyltransferase (metabolism)
• Protein Processing, Post-Translational
• Zinc (metabolism)