A nuclear RNA-binding cyclophilin in human T cells

FEBS Lett. 1996 Dec 2;398(2-3):201-5. doi: 10.1016/s0014-5793(96)01248-3.

Abstract

Cyclophilins (CyPs) are binding proteins for the immunosuppressive drug cyclosporin A (CsA). CyPs are evolutionarily highly conserved proteins present in both pro- and eukaryotes as well as in different subcellular locations. CyPs possess enzymatic activity, namely peptidyl-prolyl cis-trans isomerase (PPIase) activity; CyPs are involved in cellular protein folding and protein interactions. To date, only cyclosporins and proteins are known to interact with CyPs. Here we describe a novel nuclear cyclophilin (hCyP33) from human T cells with an additional RNA-binding domain. This combines for the first time RNA binding and protein folding in one protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Isomerases / chemistry*
  • Amino Acid Isomerases / metabolism
  • Amino Acid Sequence
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism
  • Cloning, Molecular
  • Cyclophilins*
  • DNA, Complementary
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Peptidylprolyl Isomerase
  • Protein Folding
  • RNA / metabolism*
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • T-Lymphocytes / chemistry*

Substances

  • Carrier Proteins
  • DNA, Complementary
  • Nuclear Proteins
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • RNA
  • Amino Acid Isomerases
  • Cyclophilins
  • PPIE protein, human
  • Peptidylprolyl Isomerase

Associated data

  • PIR/S66681