Barley elongation factor 1α: genomic organization, DNA sequence, and phylogenetic implications

Genome ◽  
1997 ◽  
Vol 40 (4) ◽  
pp. 559-565 ◽  
Author(s):  
Peter S. Nielsen ◽  
Andris Kleinhofs ◽  
Odd-Arne Olsen
Keyword(s):  
Amino Acid ◽  
Gene Family ◽  
Genomic Organization ◽  
Elongation Factor ◽  
Total Proteins ◽  
Elongation Factor 1Α ◽  
Barley Endosperm ◽  
Barley Cultivars ◽  
Amino Acid Sequence Comparison ◽  
Phylogenetic Implications

A full length cDNA clone encoding the 447 amino acid long barley (Hordeum vulgare cv. Bomi) endosperm elongation factor 1α (eF-1α) was isolated by a differential screening procedure. RFLP mapping of eF-1α showed that the barley genome contains a small eF-1α gene family of 4 copies, with 1 copy of the gene being located on each of chromosomes 2, 4, 6, and 7. Analysis of barley endosperm total proteins by Western blot with antibodies directed towards wheat eF-1α and the sea urchin 51 kDa proteins gave a single band of the expected molecular weight. Amino acid sequence comparison with other plant eF-1α sequences showed that the isolated barley endosperm eF-1α is more similar to the published wheat eF-1α sequence than to eF-1α sequences previously published for the barley cultivars Igri and Dicktoo. The phylogenetic analysis suggests that the barley eF-1α gene family can be divided into two subfamilies and that two ancestral genes existed before the divergence of monocotyledonous and dicotyledonous plants.Key words: endosperm, gene family, RFLP.

Genomic organization and expression of elongation factor-1α genes in Trypanosoma brucei

1996 ◽  
Vol 79 (1) ◽  
pp. 119-123 ◽  
Author(s):  
Evelyn L. Ridgley ◽  
Zhao-hui Xiong ◽  
Kiran J. Kaur ◽  
Larry Ruben
Keyword(s):  
Trypanosoma Brucei ◽  
Genomic Organization ◽  
Elongation Factor ◽  
Elongation Factor 1Α

Blastocystis elongation factor-1α: genomic organization, taxonomy and phylogenetic relationships

Parasitology ◽  
2000 ◽  
Vol 121 (2) ◽  
pp. 135-144 ◽  
Author(s):  
L. C. HO ◽  
A. ARMUGAM ◽  
K. JEYASEELAN ◽  
E. H. YAP ◽  
M. SINGH
Keyword(s):  
Phylogenetic Relationships ◽  
Genomic Organization ◽  
Elongation Factor ◽  
Elongation Factor 1Α

Nucleotide sequence of a DNA region comprising the gene for elongation factor 1α (EF-1α) from the ultrathermophilic archaeotePyrococcus woesei: Phylogenetic implications

1991 ◽  
Vol 33 (4) ◽  
pp. 332-342 ◽  
Author(s):  
Roberta Creti ◽  
Franca Citarella ◽  
Orsola Tiboni ◽  
Annamaria Sanangelantoni ◽  
Peter Palm ◽  
...  
Keyword(s):  
Nucleotide Sequence ◽  
Elongation Factor ◽  
Elongation Factor 1Α ◽  
Phylogenetic Implications

scholarly journals Retropseudogenes constitute the major part of the human elongation factor 1α gene family

1990 ◽  
Vol 18 (6) ◽  
pp. 1513-1516 ◽  
Author(s):  
Hans O. Madsen ◽  
Knud Poulsen ◽  
Otto Dahl ◽  
Brian F.C. Clark ◽  
J.Peter Hjorth
Keyword(s):  
Gene Family ◽  
Major Part ◽  
Elongation Factor ◽  
Elongation Factor 1Α ◽  
Human Elongation Factor

scholarly journals Crystal structure of human cytosolic aspartyl-tRNA synthetase

2014 ◽  
Vol 70 (a1) ◽  
pp. C1403-C1403
Author(s):  
Sang Ho Park ◽  
Kyung Rok Kim ◽  
Hyoun Sook Kim ◽  
Kyung Hee Rhee ◽  
Byung-Gyu Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amino Acid ◽  
Binding Site ◽  
Elongation Factor ◽  
Trna Synthetase ◽  
Post Translational Modification ◽  
Elongation Factor 1Α ◽  
Dimer Interface ◽  
Switching Model ◽  
Cognate Trna

Human cytosolic aspartyl-tRNA synthetase (DRS) catalyzes the attachment of the amino acid aspartic acid to its cognate tRNA and it is a component of the multi-tRNA synthetase complex (MSC) which has been known to be involved in unexpected signaling pathways. Here, we report the crystal structure of DRS at 2.25 Å resolution. DRS is a homodimer with a dimer interface 3,750.5 Å2which comprises of 16.6% of the monomeric surface area. Our structure reveals the C-terminal end of the N-helix which is considered as a unique addition in DRS, and its conformation further supports the switching model of the N-helix for the transfer of tRNAAsp to elongation factor 1α. From our analyses of the crystal structure and post-translational modification of DRS, we suggest that the phosphorylation of Ser146 provokes the separation of DRS from the MSC and provides the binding site for an interaction partner with unforeseen functions.

scholarly journals Amino Acid Sequence of Rubber Elongation Factor Protein Associated with Rubber Particles in Hevea Latex

1989 ◽  
Vol 264 (31) ◽  
pp. 18618-18626 ◽  
Author(s):  
M S Dennis ◽  
W J Henzel ◽  
J Bell ◽  
W Kohr ◽  
D R Light
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Elongation Factor ◽  
Rubber Particles

scholarly journals Methionine and Arginine Supply Alters Abundance of Amino Acid, Insulin Signaling, and Glutathione Metabolism-Related Proteins in Bovine Subcutaneous Adipose Explants Challenged with N-Acetyl-d-sphingosine

Animals ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 2114
Author(s):  
Yusheng Liang ◽  
Nana Ma ◽  
Danielle N. Coleman ◽  
Fang Liu ◽  
Yu Li ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Amino Acid ◽  
Insulin Signaling ◽  
Elongation Factor ◽  
In Vivo Studies ◽  
Glutathione Metabolism ◽  
Protein Abundance ◽  
Related Proteins ◽  
Subcutaneous Adipose

The objective was to perform a proof-of-principle study to evaluate the effects of methionine (Met) and arginine (Arg) supply on protein abundance of amino acid, insulin signaling, and glutathione metabolism-related proteins in subcutaneous adipose tissue (SAT) explants under ceramide (Ce) challenge. SAT from four lactating Holstein cows was incubated with one of the following media: ideal profile of amino acid as the control (IPAA; Lys:Met 2.9:1, Lys:Arg 2:1), increased Met (incMet; Lys:Met 2.5:1), increased Arg (incArg; Lys:Arg 1:1), or incMet plus incArg (Lys:Met 2.5:1 Lys:Arg 1:1) with or without 100 μM exogenous cell-permeable Ce (N-Acetyl-d-sphingosine). Ceramide stimulation downregulated the overall abundance of phosphorylated (p) protein kinase B (AKT), p-mechanistic target of rapamycin (mTOR), and p-eukaryotic elongation factor 2 (eEF2). Without Ce stimulation, increased Met, Arg, or Met + Arg resulted in lower p-mTOR. Compared with control SAT stimulated with Ce, increased Met, Arg, or Met + Arg resulted in greater activation of mTOR (p-mTOR/total mTOR) and AKT (p-AKT/total AKT), with a more pronounced response due to Arg. The greatest protein abundance of glutathione S-transferase Mu 1 (GSTM1) was detected in response to increased Met supply during Ce stimulation. Ceramide stimulation decreased the overall protein abundance of the Na-coupled neutral amino acid transporter SLC38A1 and branched-chain alpha-ketoacid dehydrogenase kinase (BCKDK). However, compared with controls, increased Met or Arg supply attenuated the downregulation of BCKDK induced by Ce. Circulating ceramides might affect amino acid, insulin signaling, and glutathione metabolism in dairy cow adipose tissue. Further in vivo studies are needed to confirm the role of rumen-protected amino acids in regulating bovine adipose function.

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