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Interactions of aflatoxin B 1 with SRP components can disrupt protein targeting
Author(s) -
Singh Jasbir,
Singh Suman,
Dani Harinder M.,
Sharma Rajeshwar,
Steinberg Pablo
Publication year - 2004
Publication title -
cell biochemistry and function
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.933
H-Index - 61
eISSN - 1099-0844
pISSN - 0263-6484
DOI - 10.1002/cbf.1120
Subject(s) - signal recognition particle , endoplasmic reticulum , polysome , cytoplasm , chemistry , signal peptide , aflatoxin , biophysics , biochemistry , signal recognition particle receptor , microbiology and biotechnology , ribosome , biology , peptide sequence , rna , gene , food science
Spectrofluorimetric studies have revealed that aflatoxin B 1 (AFB 1 ) interacts with signal recognition particle (SRP), which acts as an escort for polyribosomes with signal peptides to be transported and bound to the cytoplasmic face of the endoplasmic reticulum (ER). We further report that the binding of AFB 1 to SRP is selective as it only binds to two (SRP9 and 14) out of its three constituent polypeptides studied. Binding of AFB 1 to proteins is known to alter their conformations. Interactions of AFB 1 with SRP polypeptides may generate structural and functional alterations in this particle and hinder secretory protein synthesis. Copyright © 2004 John Wiley & Sons, Ltd.