Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11110%2F11%3A9171" target="_blank" >RIV/00216208:11110/11:9171 - isvavai.cz</a>
Alternative codes found
RIV/61388971:_____/11:00371869
Result on the web
<a href="http://dx.doi.org/10.1039/c0mb00174k" target="_blank" >http://dx.doi.org/10.1039/c0mb00174k</a>
DOI - Digital Object Identifier
—
Alternative languages
Result language
angličtina
Original language name
Phosphorylation of ribosomal proteins influences subunit association and translation of poly (U) in Streptomyces coelicolor
Original language description
The occurrence of phosphorylated proteins in ribosomes of Streptomyces coelicolor was investigated. Little is known about which biological functions these posttranslational modifications might fulfil. A protein kinase associated with ribosomes phosphorylated six ribosomal proteins of the small subunit (S3, S4, S12, S13, S14 and S18) and seven ribosomal proteins of the large subunit (L2, L3, L7/L12, L16, L17, L23 and L27). The ribosomal proteins were phosphorylated mainly on the Ser/Thr residues. Phosphorylation of the ribosomal proteins influences ribosomal subunits association. Ribosomes with phosphorylated proteins were used to examine poly (U) translation activity. Phosphorylation induced about 50% decrease in polyphenylalanine synthesis. After preincubation of ribosomes with alkaline phosphatase the activity of ribosomes was greatly restored. Small differences were observed between phosphorylated and unphosphorylated ribosomes in the kinetic parameters of the binding of Phe-tRNA to
Czech name
—
Czech description
—
Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EE - Microbiology, virology
OECD FORD branch
—
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Molecular BioSystems
ISSN
1742-206X
e-ISSN
—
Volume of the periodical
7
Issue of the periodical within the volume
3
Country of publishing house
GB - UNITED KINGDOM
Number of pages
7
Pages from-to
817-823
UT code for WoS article
000287367100026
EID of the result in the Scopus database
—