[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].Mol Biol (Mosk). 2001 Jul-Aug; 35(4):617-27.MB
Abstract
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.
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MeSH
Pub Type(s)
Journal Article
Language
rus
PubMed ID
11524948
Citation
Rassokhin, T I., et al. "[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]." Molekuliarnaia Biologiia, vol. 35, no. 4, 2001, pp. 617-27.
Rassokhin TI, Golovin AV, Petrova EB, et al. [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]. Mol Biol (Mosk). 2001;35(4):617-27.
Rassokhin, T. I., Golovin, A. V., Petrova, E. B., Spiridonova, V. A., Karginova, O. A., Rozhdestvenskiĭ, T. S., Brosius, J., & Kopylov, A. M. (2001). [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]. Molekuliarnaia Biologiia, 35(4), 617-27.
Rassokhin TI, et al. [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]. Mol Biol (Mosk). 2001 Jul-Aug;35(4):617-27. PubMed PMID: 11524948.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - [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].
AU - Rassokhin,T I,
AU - Golovin,A V,
AU - Petrova,E B,
AU - Spiridonova,V A,
AU - Karginova,O A,
AU - Rozhdestvenskiĭ,T S,
AU - Brosius,J,
AU - Kopylov,A M,
PY - 2001/8/30/pubmed
PY - 2002/1/17/medline
PY - 2001/8/30/entrez
SP - 617
EP - 27
JF - Molekuliarnaia biologiia
JO - Mol Biol (Mosk)
VL - 35
IS - 4
N2 - 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.
SN - 0026-8984
UR - https://www.unboundmedicine.com/medline/citation/11524948/[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]_
L2 - http://ovidsp.ovid.com/ovidweb.cgi?T=JS&PAGE=linkout&SEARCH=11524948.ui
DB - PRIME
DP - Unbound Medicine
ER -