The length of the interdomain region of the L7/L12 protein is important for its function

Bubunenko, Mikhail; Chuikov, Sergei; Gudkov, A.T.

doi:10.1016/0014-5793(92)81198-u

Cited by 19 publications

(21 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The N-terminal domain has a role in dimerization and anchoring L7/L12 to the ribosome, while the C-terminal domain interacts with the factors during translation. Finally, the hinge region, including residues 33 to 52, of L7/L12 is an alanine rich region responsible for large conformational changes of the C-terminal domain of the protein during translocation 30,64-66. Recently, requirement of L7/L12 phosphorylation and acetylation for ribosome association was demonstrated by mass spectrometry; however, the specific sites for phosphorylation were not determined 17,67.…”

Section: Resultsmentioning

confidence: 99%

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

et al. 2009

View full text Add to dashboard Cite

Phosphorylation of bacterial ribosomal proteins has been known for decades; however, there is still very limited information available on specific locations of the phosphorylation sites in ribosomal proteins and the role they might play in protein synthesis. In this study, we have mapped the specific phosphorylation sites in twenty-four E. coli ribosomal proteins by tandem mass spectrometry. Specific detection of phosphorylation was achieved by either phosphorylation specific visualization techniques, ProQ staining and antibodies for phospho-Ser, Thr, and Tyr, or by mass spectrometry equipped with a capability to detect addition and the loss of the phosphate moiety. Enrichment by immobilized metal affinity and/or strong cation exchange chromatography was used to improve the success of detection of the low abundance phosphopeptides. We found the small subunit (30S) proteins S3, S4, S5, S7, S11, S12, S13, S18, and S21 and the large subunit (50S) proteins L1, L2, L3, L5, L6, L7/L12, L13, L14, L16, L18, L19, L21, L22, L28, L31 to be phosphorylated at one or more residues. Potential roles for each specific site in ribosome function were deduced through careful evaluation of the given site of the phosphorylation in 3D-crystal structure models of ribosomes and the previous mutational studies of E. coli ribosomal proteins.

show abstract

Section: Resultsmentioning

confidence: 99%

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

et al. 2009

View full text Add to dashboard Cite

show abstract

“…Considering the data cited above, we can conclude that formation of the S-S bond in the mutant protein does not influence the flexibility of the hinge region (residues 38-50), which is functionally important [18,19] and does not distort the structure of the N-terminal sequence which is responsible for protein dimerization [4,6].…”

Section: Resultsmentioning

confidence: 99%

The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein

1995

Self Cite

View full text Add to dashboard Cite

show abstract

“…The deletion of amino acids from the hinge has a more pronounced effect than their insertion [50]. Reconstitution of 50S subunits deprived of wild type L7/L12 with deletion mutants Δ44–52 and Δ38–52 produce virtually inactive ribosomes, while the insertion mutant (with 14 added amino acids) give functionally active subunits.…”

Section: Functional Studiesmentioning

confidence: 99%

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

Gudkov

1997

FEBS Letters

Self Cite

View full text Add to dashboard Cite

The L7/L12 protein forms a functionally important domain in the ribosome. This domain is involved in interaction with translation factors during protein biosynthesis. The tertiary and quaternary structure of the L7/L12 protein was established as a result of intensive studies in solution and in the ribosome. The conformational changes of L7/L12, the elongation factors Tu and G and other ribosomal proteins were traced by different experimental techniques. These changes occur upon interaction of the ribosome with the elongation factors and depend on GTP hydrolysis in accordance with the functional states of the ribosome.

show abstract

The length of the interdomain region of the L7/L12 protein is important for its function

Abstract: Several mutated L7/LI2 proteins with changed intcrdomain regions were obtained. The results showed that tile flexible region comprising the 39-52 amino acid residues is functionally important. Its length, but not its amino acid composition, is crucial for the function.

Cited by 19 publications

References 24 publications

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

Comprehensive Analysis of Phosphorylated Proteins of Escherichia coli Ribosomes

The first 37 residues are sufficient for dimerization of ribosomal L7/L12 protein

The L7/L12 ribosomal domain of the ribosome: structural and functional studies

Contact Info

Product

Resources

About