scholarly journals The N-terminal domain (IF2N) of bacterial translation initiation factor IF2 is connected to the conserved C-terminal domains by a flexible linker

2004 ◽  
Vol 13 (1) ◽  
pp. 230-239 ◽  
Author(s):  
B. S. Laursen
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Terminal Domain ◽  
Bacterial Translation Initiation ◽  
Bacterial Translation ◽  
Terminal Domains

scholarly journals A Conserved Structural Motif at the N Terminus of Bacterial Translation Initiation Factor IF2

2003 ◽  
Vol 278 (18) ◽  
pp. 16320-16328 ◽  
Author(s):  
Brian Søgaard Laursen ◽  
Kim Kusk Mortensen ◽  
Hans Uffe Sperling-Petersen ◽  
David W. Hoffman
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Structural Motif ◽  
Initiation Factor ◽  
N Terminus ◽  
Bacterial Translation Initiation ◽  
Bacterial Translation

Mapping the Active Sites of Bacterial Translation Initiation Factor IF3

2003 ◽  
Vol 331 (3) ◽  
pp. 541-556 ◽  
Author(s):  
Dezemona Petrelli ◽  
Cristiana Garofalo ◽  
Matilde Lammi ◽  
Roberto Spurio ◽  
Cynthia L Pon ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Active Sites ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Bacterial Translation Initiation ◽  
Bacterial Translation

scholarly journals Structural Dynamics of Bacterial Translation Initiation Factor IF2

2012 ◽  
Vol 287 (14) ◽  
pp. 10922-10932 ◽  
Author(s):  
Hans Wienk ◽  
Evgeny Tishchenko ◽  
Riccardo Belardinelli ◽  
Simona Tomaselli ◽  
Ramachandra Dongre ◽  
...  
Keyword(s):  
Structural Dynamics ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Bacterial Translation Initiation ◽  
Bacterial Translation

scholarly journals In silico analysis of bacterial translation factors reveal distinct translation event specific pI values

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Soma Jana ◽  
Partha P. Datta
Keyword(s):  
Translation Initiation ◽  
In Silico ◽  
Bacterial Species ◽  
Amino Acid Sequences ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Release Factors ◽  
Translation Factors ◽  
70S Ribosome ◽  
Bacterial Translation

Abstract Background Protein synthesis is a cellular process that takes place through the successive translation events within the ribosome by the event-specific protein factors, namely, initiation, elongation, release, and recycling factors. In this regard, we asked the question about how similar are those translation factors to each other from a wide variety of bacteria? Hence, we did a thorough in silico study of the translation factors from 495 bacterial sp., and 4262 amino acid sequences by theoretically measuring their pI and MW values that are two determining factors for distinguishing individual proteins in 2D gel electrophoresis in experimental procedures. Then we analyzed the output from various angles. Results Our study revealed the fact that it’s not all same, or all random, but there are distinct orders and the pI values of translation factors are translation event specific. We found that the translation initiation factors are mainly basic, whereas, elongation and release factors that interact with the inter-subunit space of the intact 70S ribosome during translation are strictly acidic across bacterial sp. These acidic elongation factors and release factors contain higher frequencies of glutamic acids. However, among all the translation factors, the translation initiation factor 2 (IF2) and ribosome recycling factor (RRF) showed variable pI values that are linked to the order of phylogeny. Conclusions From the results of our study, we conclude that among all the bacterial translation factors, elongation and release factors are more conserved in terms of their pI values in comparison to initiation and recycling factors. Acidic properties of these factors are independent of habitat, nature, and phylogeny of the bacterial species. Furthermore, irrespective of the different shapes, sizes, and functions of the elongation and release factors, possession of the strictly acidic pI values of these translation factors all over the domain Bacteria indicates that the acidic nature of these factors is a necessary criterion, perhaps to interact into the partially enclosed rRNA rich inter-subunit space of the translating 70S ribosome.

scholarly journals The C-Terminal Region of Eukaryotic Translation Initiation Factor 3a (eIF3a) Promotes mRNA Recruitment, Scanning, and, Together with eIF3j and the eIF3b RNA Recognition Motif, Selection of AUG Start Codons

2010 ◽  
Vol 30 (18) ◽  
pp. 4415-4434 ◽  
Author(s):  
Wen-Ling Chiu ◽  
Susan Wagner ◽  
Anna Herrmannová ◽  
Laxminarayana Burela ◽  
Fan Zhang ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Rna Recognition Motif ◽  
Rna Recognition ◽  
Eukaryotic Translation Initiation Factor ◽  
Eukaryotic Translation ◽  
Recognition Motif ◽  
Terminal Domain ◽  
Eukaryotic Translation Initiation

ABSTRACT The C-terminal domain (CTD) of the a/Tif32 subunit of budding yeast eukaryotic translation initiation factor 3 (eIF3) interacts with eIF3 subunits j/Hcr1 and b/Prt1 and can bind helices 16 to 18 of 18S rRNA, suggesting proximity to the mRNA entry channel of the 40S subunit. We have identified substitutions in the conserved Lys-Glu-Arg-Arg (KERR) motif and in residues of the nearby box6 element of the a/Tif32 CTD that impair mRNA recruitment by 43S preinitiation complexes (PICs) and confer phenotypes indicating defects in scanning and start codon recognition. The normally dispensable CTD of j/Hcr1 is required for its binding to a/Tif32 and to mitigate the growth defects of these a/Tif32 mutants, indicating physical and functional interactions between these two domains. The a/Tif32 CTD and the j/Hcr1 N-terminal domain (NTD) also interact with the RNA recognition motif (RRM) in b/Prt1, and mutations in both subunits that disrupt their interactions with the RRM increase leaky scanning of an AUG codon. These results, and our demonstration that the extreme CTD of a/Tif32 binds to Rps2 and Rps3, lead us to propose that the a/Tif32 CTD directly stabilizes 43S subunit-mRNA interaction and that the b/Prt1-RRM-j/Hcr1-a/Tif32-CTD module binds near the mRNA entry channel and regulates the transition between scanning-conducive and initiation-competent conformations of the PIC.

scholarly journals In silico analysis of bacterial translation factors reveal distinct translation event specific pI values

2020 ◽  
Author(s):  
SOMA JANA ◽  
Partha Pratim Datta
Keyword(s):  
Translation Initiation ◽  
In Silico ◽  
Bacterial Species ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Acidic Property ◽  
Release Factors ◽  
Translation Factors ◽  
70S Ribosome ◽  
Bacterial Translation

Abstract Background Protein synthesis is a cellular process that takes place through the successive translation events within the ribosome with the help of the event-specific protein factors, namely, initiation, elongation, release, and recycling factors. The translation process is fundamental to all organisms living in the wide variety of environments. In this regard, we asked the questions about how similar are those translation factors to each other from a wide variety of bacteria? Hence, we did a thorough in silico study of the translation factors from 495 bacterial sp., and 4262 amino acid sequences, wherein we theoretically measured their pI and MW values that are the two determining factors for distinguishing individual proteins in 2D gel electrophoresis. Then we analyzed the output from various angles. Results Our study revealed that, not all the pI values are same or random, but there is a distinct order, such that the pI values of translation factors are translation event specific. We found that the translation initiation factors are mainly basic, whereas, elongation and release factors that interact with the inter-subunit space of the intact 70S ribosome during translation are strictly acidic. Further analysis revealed that the acidic property of those factors is due to the higher frequencies of glutamic acids. However, two translation factors, the translation initiation factor 2 (IF2) and the ribosome recycling factor (RRF) showed variable pI values. Remarkably, the variability of the pI values of these two factors showed distinct lineage with the order of phylogeny. Conclusion From our results we conclude that, among all the bacterial translation factors, elongation and release factors are more conserved in terms of their pI values in comparison to initiation and recycling factors. Acidic properties of these factors are independent of habitat, nature, or the phylogeny of the bacterial species. Furthermore; irrespective of the different shapes, sizes, and functions of the elongation and release factors, possession of their strictly acidic pI values indicate that the acidic nature of these factors is a necessary criterion, perhaps to interact into the partially enclosed rRNA rich inter-subunit space of the translating 70S ribosome.

scholarly journals mTORC1 induces eukaryotic translation initiation factor 4E interaction with TOS-S6 kinase 1 and its activation

2020 ◽  
Author(s):  
Sheikh Tahir Majeed ◽  
Asiya Batool ◽  
Rabiya Majeed ◽  
Nadiem Nazir Bhat ◽  
Khurshid Iqbal Andrabi
Keyword(s):  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
S6 Kinase ◽  
Eukaryotic Translation Initiation Factor ◽  
Eukaryotic Translation ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Eukaryotic Translation Initiation ◽  
Carboxy Terminal

AbstractEukaryotic translation initiation factor 4E was recently shown to be a substrate of mTORC1, suggesting it may be a mediator of mTORC1 signaling. Here, we present evidence that eIF4E phosphorylated at S209 interacts with TOS motif of S6 Kinase1 (S6K1). We also show that this interaction is sufficient to overcome rapamycin sensitivity and mTORC1 dependence of S6K1. Furthermore, we show that eIF4E-TOS interaction relieves S6K1 from auto-inhibition due to carboxy terminal domain (CTD) and primes it for hydrophobic motif (HM) phosphorylation and activation in mTORC1 independent manner. We conclude that the role of mTORC1 is restricted to engaging eIF4E with S6K1-TOS motif to influence its state of HM phosphorylation and inducing its activation.HighlightsPhosphorylated eIF4E interacts with TOS motif of S6 Kinase1eIF4E-TOS interaction relieves S6 Kinase 1 from carboxy terminal domain auto-inhibition and primes it for activation.

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