[Study of the binding of the S7 protein with 16S rRNA fragment 926-986/1219-1393 as a key step in the assembly of the small subunit of prokaryotic ribosomes].
Both structural and thermodynamic studies are necessary to understand the ribosome assembly. An initial step was made in studying the interaction between a 16S rRNA fragment and S7, a key protein in assembling the prokaryotic ribosome small subunit. The apparent dissociation constant was obtained for complexes of recombinant Escherichia coli and Thermus thermophilus S7 with a fragment of the 3' domain of the E. coli 16S rRNA. Both proteins showed a high rRNA-binding activity, which was not observed earlier. Since RNA and proteins are conformationally labile, their folding must be considered to correctly describe the RNA-protein interactions.
Rassokhin
T I
TI
Biology Departament, University of Virginia, Charlottesville, VA 22904-4775, USA.
Golovin
A V
AV
Petrova
E B
EB
Spiridonova
V A
VA
Karginova
O A
OA
Rozhdestvenskiĭ
T S
TS
Brosius
J
J
Kopylov
A M
AM
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D011487:Protein Conformation; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism; D012336:RNA, Ribosomal, 16S / Q000235:genetics / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism*; D016963:Thermus thermophilus / Q000235:genetics / Q000378:metabolism
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012336:RNA, Ribosomal, 16S; D011994:Recombinant Proteins; D012269:Ribosomal Proteins; C037442:ribosomal protein S7
Izuchenie sviazyvanie belka S7 s fragmentom 926-986/1219-1393 16S rRNK--kliuchevogo étapa sborki maloĭ subchastitsy prokarioticheskikh ribosom.