Format

Send to

Choose Destination
See comment in PubMed Commons below
J Biol Chem. 1994 Jan 14;269(2):1091-8.

IFP 35 is an interferon-induced leucine zipper protein that undergoes interferon-regulated cellular redistribution.

Author information

  • 1Institut für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, Germany.

Abstract

We have isolated a new human cDNA, named IFP 35, whose expression is regulated by interferons (IFN). Induction of IFP 35 mRNA in HeLa cells by IFN is due, at least in part, to increased transcription. In response to IFN treatment, the expression of IFP 35 mRNA is seen in a wide range of different cell types, including fibroblasts, macrophages, and epithelial cells. The cDNA sequence encodes a 282-amino acid protein with a deduced molecular mass of 31,130 Da. In vitro translation of mRNA obtained by both in vitro transcription and hybrid selection resulted in the synthesis of a 35-kDa protein. Antisera raised against IFP 35 recognized a protein with an apparent molecular mass of 35 kDa in HeLa cells. Amino acid sequence analysis revealed a leucine zipper motif in an alpha-helical configuration at the extreme amino terminus of IFP 35. Notable IFP 35 is a unique novel leucine zipper protein in that it lacks a basic domain critical for DNA binding. IFP 35 can specifically form homodimers in vitro. Western blot analysis of fractionated cell extracts indicates increased nuclear localization following IFN treatment.

PMID:
8288566
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Support Center