scholarly journals A Conserved Proline Triplet in Val-tRNA Synthetase and the Origin of Elongation Factor P

Cell Reports ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. 476-483 ◽  
Author(s):  
Agata L. Starosta ◽  
Jürgen Lassak ◽  
Lauri Peil ◽  
Gemma C. Atkinson ◽  
Christopher J. Woolstenhulme ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Elongation Factor P

scholarly journals The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

2011 ◽  
Vol 7 (10) ◽  
pp. 667-669 ◽  
Author(s):  
Hervé Roy ◽  
S Betty Zou ◽  
Tammy J Bullwinkle ◽  
Benjamin S Wolfe ◽  
Marla S Gilreath ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Elongation Factor P

A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P

2010 ◽  
Vol 17 (9) ◽  
pp. 1136-1143 ◽  
Author(s):  
Tatsuo Yanagisawa ◽  
Tomomi Sumida ◽  
Ryohei Ishii ◽  
Chie Takemoto ◽  
Shigeyuki Yokoyama
Keyword(s):  
Elongation Factor ◽  
Trna Synthetase ◽  
Lysine Residue ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Elongation Factor P

Identification of binding partners of CsaA - an archaeal chaperonic pro-tein of Picrophilus torridus

2020 ◽  
Vol 27 ◽  
Author(s):  
Neelja Singhal ◽  
Archana Sharma ◽  
Manisha Aswal ◽  
Nirpendra Singh ◽  
Manish Kumar ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Citrate Synthase ◽  
Elongation Factor ◽  
Trna Synthetase ◽  
Strong Interactions ◽  
Beta Chain ◽  
Protein Protein Interactions ◽  
Uncharacterized Protein ◽  
Binding Partners ◽  
Picrophilus Torridus

Background:: CsaA is among the few chaperones which are present in both bacteria and archaea, but absent in eukaryotes. There are no reports on interactome analysis of CsaA from archaea, till date. Identification of binding partners of CsaA might be helpful in understanding CsaA-associated processes in Picrophilus torridus– an extreme thermoaci-dophilic euryarchaeon. Objectives:: The present study was conducted to identify the binding partners of CsaA of P. torridus (PtCsaA). Methods:: The binding partners of PtCsaA were isolated and identified using a pull down assay and liquid chromatography-mass spectrometry (LC-MS). Results:: The results revealed twelve potential binding partners of CsaA. These were thermosome subunits (Q6KZS2 and Q6L132), nascent polypeptide-associated complex protein (Q6L1N3), elongation factor 1-alpha (Q6L202), uncharacterized protein (Q6L0Y6), citrate synthase (Q6L0M8), asparaginyl-tRNA synthetase (Q6L0M5), succinyl-CoA synthetase beta chain (Q6L0B4), pyruvate ferredoxin oxidoreductase alpha and beta chain proteins (Q6KZA7 and Q6KZA6, respectively), malate dehydrogenase (Q6L0C3) and reversed fumarylacetoacetase (Q6KZ97). Functional categorization revealed that of these, six proteins were involved in energy metabolic pathways, three were archaeal chaperones, two were involved in trans-lation and one might be a transcription regulator. STRING-based analysis of the protein-protein interactions of the experi-mental interactome revealed strong interactions among them. Conclusion:: PtCsaA might be a multifaceted protein which besides translation might also play important role in metabolic processes of P. torridus. However, further experiments investigating the binding partners of CsaA in other archaea are re-quired for a better understanding of CsaA-associated processes in archaea.

scholarly journals Rhizobium tropici Genes Involved in Free-Living Salt Tolerance are Required for the Establishment of Efficient Nitrogen-Fixing Symbiosis with Phaseolus vulgaris

2002 ◽  
Vol 15 (3) ◽  
pp. 225-232 ◽  
Author(s):  
Joaquina Nogales ◽  
Rosario Campos ◽  
Hanaa BenAbdelkhalek ◽  
José Olivares ◽  
Carmen Lluch ◽  
...  
Keyword(s):  
Salt Tolerance ◽  
Phaseolus Vulgaris ◽  
Environmental Changes ◽  
Nitrogenase Activity ◽  
Regulation Of Gene Expression ◽  
Elongation Factor ◽  
Regulatory System ◽  
Trna Synthetase ◽  
Nitrogen Fixing ◽  
Rhizobium Tropici

Characterization of nine transposon-induced mutants of Rhizobium tropici with decreased salt tolerance (DST) allowed the identification of eight gene loci required for adaptation to high external NaCl. Most of the genes also were involved in adaptation to hyperosmotic media and were required to overcome the toxicity of LiCl. According to their possible functions, genes identified could be classified into three groups. The first group included two genes involved in regulation of gene expression, such as ntrY, the sensor element of the bacterial ntrY/ntrX two-component regulatory system involved in regulation of nitrogen metabolism, and greA, which encodes a transcription elongation factor. The second group included genes related to synthesis, assembly, or maturation of proteins, such as alaS coding for alanine-tRNA synthetase, dnaJ, which encodes a molecular chaperone, and a nifS homolog probably encoding a cysteine desulfurase involved in the maturation of Fe-S proteins. Genes related with cellular build-up and maintenance were in the third group, such as a noeJ-homolog, encoding a mannose-1-phosphate guanylyltransferase likely involved in lipopolysaccharide biosynthesis, and kup, specifying an inner-membrane protein involved in potassium uptake. Another gene was identified that had no homology to known genes but that could be conserved in other rhizobia. When inoculated on Phaseolus vulgaris growing under nonsaline conditions, all DST mutants displayed severe symbiotic defects: ntrY and noeJ mutants were impaired in nodulation, and the remaining mutants formed symbiosis with very reduced nitrogenase activity. The results suggest that bacterial ability to adapt to hyper-osmotic and salt stress is important for the bacteroid nitrogen-fixing function inside the legume nodule and provide genetic evidence supporting the suggestion that rhizobia face severe environmental changes after their release into plant cells.

Protein translation components are colocalized in granules in oligodendrocytes

1995 ◽  
Vol 108 (8) ◽  
pp. 2781-2790 ◽  
Author(s):  
E. Barbarese ◽  
D.E. Koppel ◽  
M.P. Deutscher ◽  
C.L. Smith ◽  
K. Ainger ◽  
...  
Keyword(s):  
Myelin Basic Protein ◽  
Ribosomal Rna ◽  
Spatial Organization ◽  
Basic Protein ◽  
Elongation Factor ◽  
Protein Translation ◽  
Trna Synthetase ◽  
Laser Scanning Microscopy ◽  
Dual Channel ◽  
Cross Correlation Analysis

The intracellular distribution of various components of the protein translational machinery was visualized in mouse oligodendrocytes in culture using high resolution fluorescence in situ hybridization and immunofluorescence in conjunction with dual channel confocal laser scanning microscopy. Arginyl-tRNA synthetase, elongation factor 1a, ribosomal RNA, and myelin basic protein mRNA were all co-localized in granules in the processes, veins and membrane sheets of the cell. Colocalization was evaluated by dual channel cross correlation analysis to determine the correlation index (% colocalization) and correlation distance (granule radius), and by single granule ratiometric analysis to determine the distribution of the different components in individual granules. Most granules contained synthetase, elongation factor, ribosomal RNA and myelin basic protein mRNA. These results indicate that several different components of the protein synthetic machinery, including aminoacyl-tRNA synthetases, elongation factors, ribosomes and mRNAs, are colocalized in granules in oligodendrocytes. We propose that these granules are supramolecular complexes containing all of the necessary macromolecular components for protein translation and that they represent a heretofore undescribed subcellular organization of the protein synthetic machinery. This spatial organization may increase the efficiency of protein synthesis and may also provide a vehicle for transport and localization of specific mRNAs within the cell.

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