A newly isolated Pex7-binding, atypical PTS2 protein P7BP2 is a novel dynein-type AAA+ protein
Author(s) -
Hajime Niwa,
Yasuhiro Miyauchi-Nanri,
Kanji Okumoto,
Satoru Mukai,
Kentaro Noi,
Teru Ogura,
Yukio Fujiki
Publication year - 2018
Publication title -
the journal of biochemistry
Language(s) - Hungarian
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 115
eISSN - 1756-2651
pISSN - 0021-924X
DOI - 10.1093/jb/mvy073
Subject(s) - peroxisome , peroxisomal targeting signal , chemistry , homology (biology) , gene isoform , organelle , size exclusion chromatography , protein structure , biochemistry , peptide sequence , biology , biophysics , enzyme , receptor , amino acid , gene
A newly isolated binding protein of peroxisomal targeting signal type 2 (PTS2) receptor Pex7, termed P7BP2, is transported into peroxisomes by binding to the longer isoform of Pex5p, Pex5pL, via Pex7p. The binding to Pex7p and peroxisomal localization of P7BP2 depends on the cleavable PTS2 in the N-terminal region, suggesting that P7BP2 is a new PTS2 protein. By search on human database, three AAA+ domains are found in the N-terminal half of P7BP2. Protein sequence alignment and motif search reveal that in the C-terminal region P7BP2 contains additional structural domains featuring weak but sufficient homology to AAA+ domain. P7BP2 behaves as a monomer in gel-filtration chromatography and the single molecule observed under atomic force microscope shapes a disc-like ring. Collectively, these results suggest that P7BP2 is a novel dynein-type AAA+ family protein, of which domains are arranged into a pseudo-hexameric ring structure.
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