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Conformational independence of N‐ and C‐domains in ribosomal protein L7/L12 and in the complex with protein L10
Author(s) -
Bocharov E.V,
Gudkov A.T,
Budovskaya E.V,
Arseniev A.S
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00121-5
Subject(s) - ribosomal protein , chemistry , independence (probability theory) , ribosome , biochemistry , rna , gene , statistics , mathematics
Isolated N‐ (1–37) and C‐terminal (47–120) fragments of L7 protein, and pentameric (L7) 4 L10 complex were studied by NMR spectroscopy in solution. The results indicate that the dimer state of the 1–37 fragment with a helical hairpin conformation is identical to the N‐terminal structure of the intact L7 dimer. The C‐terminal domain of the L7 protein does not participate in (L7) 4 L10 complex formation. The overall motions of the L7 C‐domains are essentially independent both in the L7 dimer and in the (L7) 4 L10 complex. Conformational motions on a millisecond time scale are detected in the (L7) 4 L10 complex. The possible relevance of these motions to the biological function of L7/L12 is discussed.