Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/53821
Type: Artigo de periódico
Title: A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57
Author: Nery, FC
Bressan, GC
Alborghetti, MR
Passos, DO
Kuniyoshi, TM
Ramos, CHI
Oyama, S
Kobarg, J
Abstract: Ki-1/57 is a 57-kDa cytoplasmic and nuclear protein associated with protein kinase activity and is hyper-phosphorylated on Ser/Thr residues upon cellular activation. In previous studies we identified the receptor of activated kinase-1 (RACK1), a signaling adaptor protein that binds activated PKC, as a protein that interacts with Ki-1/57. Here we demonstrate that the far-UV circular dichroism spectrum of the WD repeat-containing RACK1 protein shows an unusual positive ellipticity at 229 nm, which in other proteins of the WD family has been attributed to surface tryptophans that are quenchable by N-bromo-succinimide (NBS). As well as NBS, in vitro binding of 6xHis-Ki-1/57(122-413) and 6xHis-Ki-1/57(264-413) can also quench the positive ellipticity of the RACK1 spectrum. We generated a model of RACK1 by homology modeling using a G protein beta subunit as template. Our model suggests the family-typical seven-bladed beta-propeller, with an aromatic cluster around the central tunnel that contains four Trp residues (17, 83, 150, 170), which are likely involved in the interaction with Ki-1/57.
Subject: circular dichroism
emission fluorescence
molecular modeling
protein-protein interaction
regulatory proteins
surface tryptophans
Country: Alemanha
Editor: Walter De Gruyter & Co
Rights: embargo
Identifier DOI: 10.1515/BC.2006.074
Date Issue: 2006
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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