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- Title
Molecular determinants of Drosophila immunophilin FKBP39 nuclear localization.
- Authors
Orłowski, Marek; Popławska, Katarzyna; Pieprzyk, Joanna; Szczygieł-Sommer, Aleksandra; Więch, Anna; Zarębski, Mirosław; Tarczewska, Aneta; Dobrucki, Jurek; Ożyhar, Andrzej
- Abstract
FK506-binding proteins (FKBPs) belong to a distinct class of immunophilins that interact with immunosuppressants. They use their peptidyl-prolyl isomerase (PPIase) activity to catalyze the cis-trans conversion of prolyl bonds in proteins during protein-folding events. FKBPs also act as a unique group of chaperones. The Drosophila melanogaster peptidyl-prolyl cis-trans isomerase FK506-binding protein of 39 kDa (FKBP39) is thought to act as a transcriptional modulator of gene expression in 20-hydroxyecdysone and juvenile hormone signal transduction. The aim of this study was to analyze the molecular determinants responsible for the subcellular distribution of an FKBP39-yellow fluorescent protein (YFP) fusion construct (YFP-FKBP39). We found that YFPFKBP39 was predominantly nucleolar. To identify the nuclear localization signal (NLS), a series of YFP-tagged FKBP39 deletion mutants were prepared and examined in vivo. The identified NLS signal is located in a basic domain. Detailed mutagenesis studies revealed that residues K188 and K191 are crucial for the nuclear targeting of FKBP39 and its nucleoplasmin-like (NPL) domain contains the sequence that controls the nucleolar-specific translocation of the protein. These results show that FKBP39 possesses a specific NLS in close proximity to a putative helix-turn-helix (HTH) motif and FKBP39 may bind DNA in vivo and in vitro.
- Subjects
CARRIER proteins; DROSOPHILA; IMMUNOPHILINS; IMMUNOSUPPRESSION; IMMUNOSUPPRESSIVE agents; YELLOW fluorescent protein
- Publication
Biological Chemistry, 2018, Vol 399, Issue 5, p467
- ISSN
1431-6730
- Publication type
Article
- DOI
10.1515/hsz-2017-0251