title: Investigation of Structure of the Ribosomal L12/P Stalk.
abstract: This review contains recent data on the structure of the functionally important ribosomal domain, L12/P stalk, of the large ribosomal subunit. It is the most mobile site of the ribosome; it has been found in ribosomes of all living cells, and it is involved in the interaction between ribosomes and translation factors. The difference between the structures of the ribosomal proteins forming this protuberance (despite their general resemblance) determines the specificity of interaction between eukaryotic and prokaryotic ribosomes and the respective protein factors of translation. In this review, works on the structures of ribosomal proteins forming the L12/P-stalk in bacteria, archaea, and eukaryotes and data on structural aspects of interactions between these proteins and rRNA are described in detail.
authors.affiliation: Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia. garber@vega.protres.ru.
authors.forename: I V
authors.initials: IV
authors.lastname: Mitroshin
authors.forename: M B
authors.initials: MB
authors.lastname: Garber
authors.forename: A G
authors.initials: AG
authors.lastname: Gabdulkhakov
mesh_terms: D000818:Animals; D020285:Cryoelectron Microscopy; D056890:Eukaryota / Q000166:cytology / Q000502:physiology; D006801:Humans; D011387:Prokaryotic Cells; D014176:Protein Biosynthesis; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry*
chemical_list: D012269:Ribosomal Proteins