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Dynamics of group II chaperonin and prefoldin probed by 13 C NMR spectroscopy
Author(s) -
Kurimoto Eiji,
Nishi Yohei,
Yamaguchi Yoshiki,
Zako Tamotsu,
Iizuka Ryo,
Ide Naoki,
Yohda Masafumi,
Kato Koichi
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.21606
Subject(s) - chemistry , molecular dynamics , chaperonin , nuclear magnetic resonance spectroscopy , crystallography , biophysics , folding (dsp implementation) , stereochemistry , protein folding , biochemistry , biology , computational chemistry , electrical engineering , engineering
Group II chaperonin (CPN) cooperates with prefoldin (PFD), which forms a jellyfish‐shaped heterohexameric complex with a molecular mass of 87 kDa. PFD captures an unfolded protein with the tentacles and transfers it to the cavity of CPN. Although X‐ray crystal structures of CPN and PFD have been reported, no structural information has been so far available for the terminal regions of the PFD tentacles nor for the C‐terminal segments of CPNs, which were regarded to be functionally significant in the previous studies. Here we report 13 C NMR analyses on archaeal PFD, CPN, and their complex, focusing on those structurally uncharacterized regions. The PFD and CPN complexes selectively labeled with 13 C at methionyl carbonyl carbons were separately and jointly subjected to NMR measurements. 13 C NMR spectral data demonstrated that the N‐terminal segment of the α and β subunits of PFD as well as the C‐terminal segments of the CPN hexadecamer retain significant degrees of freedom in internal motion even in the complex with a molecular mass of 1.1 MDa. Proteins 2008. © 2007 Wiley‐Liss, Inc.