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Role of different regions of ribosomal proteins L7 and L10 in their complex formation and in the interaction with the ribosomal 50 S subunit
Author(s) -
Gudkov A.T.,
Tumanova L.G.,
Gongadze G.M.,
Bushuev V.N.
Publication year - 1980
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 - 10.1016/0014-5793(80)81305-6
Subject(s) - ribosomal protein , eukaryotic large ribosomal subunit , ribosomal rna , protein subunit , eukaryotic small ribosomal subunit , 30s , ribosome , chemistry , biology , 18s ribosomal rna , biochemistry , rna , gene
It has been shown recently that ribosomal proteins L7 and LlO form a stable complex with each other in solution [ 1,2]. A tertiary and quaternary structure has been proposed for the protein L7 [3]. The stoichiometry of the complex between the proteins L7 and LlO have been determined and some of its physical characteristics studied [4,5]. This paper presents the results of further physicochemical studies of the (L7).,.LlO complex. The conclusions are drawn that: (1) The N-terminal regions of the protein L7 which are responsible for its dimerization also participate in the binding with the protein LlO; (2) The C-terminal sequence 71-165 of the protein LlO binds all the 4 copies of the protein L7; (3) Cys-70 of the protein LIO is easily accessible to modifying agents both in the free protein and in the (L7)4.L10 complex; (4) The N-terminal sequence l-69 of the protein LlO participates in the binding of the (L7),.LlO complex with the ribosome.