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A nuclear RNA‐binding cyclophilin in human T cells
Author(s) -
Mi Huaifeng,
Kops Oliver,
Zimmermann Esther,
Jäschke Anja,
Tropschug Maximilian
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01248-3
Subject(s) - cyclophilin , cyclophilin a , microbiology and biotechnology , rna , chemistry , biophysics , computational biology , biology , biochemistry , gene
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.