title: Domain I of ribosomal protein L1 is sufficient for specific RNA binding.
abstract: Ribosomal protein L1 has a dual function as a ribosomal protein binding 23S rRNA and as a translational repressor binding its mRNA. L1 is a two-domain protein with N- and C-termini located in domain I. Earlier it was shown that L1 interacts with the same targets on both rRNA and mRNA mainly through domain I. We have suggested that domain I is necessary and sufficient for specific RNA-binding by L1. To test this hypothesis, a truncation mutant of L1 from Thermus thermophilus, representing domain I, was constructed by deletion of the central part of the L1 sequence, which corresponds to domain II. It was shown that the isolated domain I forms stable complexes with specific fragments of both rRNA and mRNA. The crystal structure of the isolated domain I was determined and compared with the structure of this domain within the intact protein L1. This comparison revealed a close similarity of both structures. Our results confirm our suggestion that in protein L1 its domain I alone is sufficient for specific RNA binding, whereas domain II stabilizes the L1-rRNA complex.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow region, Russia.
authors.forename: Svetlana
authors.initials: S
authors.lastname: Tishchenko
authors.forename: Ekaterina
authors.initials: E
authors.lastname: Nikonova
authors.forename: Vladislav
authors.initials: V
authors.lastname: Kljashtorny
authors.forename: Olga
authors.initials: O
authors.lastname: Kostareva
authors.forename: Natalia
authors.initials: N
authors.lastname: Nevskaya
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Piendl
authors.forename: Natalia
authors.initials: N
authors.lastname: Davydova
authors.forename: Victor
authors.initials: V
authors.lastname: Streltsov
authors.forename: Maria
authors.initials: M
authors.lastname: Garber
authors.forename: Stanislav
authors.initials: S
authors.lastname: Nikonov
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001665:Binding Sites; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism*; D012338:RNA, Ribosomal, 23S / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism; D016963:Thermus thermophilus
chemical_list: D001426:Bacterial Proteins; D012333:RNA, Messenger; D012338:RNA, Ribosomal, 23S; D012269:Ribosomal Proteins; C028546:ribosomal protein L1