scholarly journals Amino Acid Sequence of an Algal Peptide Elongation Factor EF-2 Deduced from the Complementary DNA Sequence

1991 ◽  
Vol 97 (1) ◽  
pp. 469-471 ◽  
Author(s):  
Gabriele Schnelbögl ◽  
Widmar Tanner
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequence ◽  
Elongation Factor ◽  
Complementary Dna ◽  
Peptide Elongation

Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence

Nature ◽  
1985 ◽  
Vol 316 (6030) ◽  
pp. 696-700 ◽  
Author(s):  
David H. MacLennan ◽  
Christopher J. Brandl ◽  
Bozena Korczak ◽  
N. Michael Green
Keyword(s):  
Amino Acid ◽  
Sarcoplasmic Reticulum ◽  
Amino Acid Sequence ◽  
Dna Sequence ◽  
Rabbit Muscle ◽  
Complementary Dna ◽  
Dependent Atpase

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 DNA sequence of the E.coli trpR gene and prediction of the amino acid sequence of Trp repressor

1980 ◽  
Vol 8 (7) ◽  
pp. 1551-1560 ◽  
Author(s):  
C.K. Singleton ◽  
W.D. Roeder ◽  
Gregg Bogosian ◽  
R.L. Somerville ◽  
H.L. Weith
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dna Sequence ◽  
Trp Repressor

Phylogenetic depth ofThermotoga maritima inferred from analysis of thefus gene: Amino acid sequence of elongation factor G and organization of theThermotoga str operon

1991 ◽  
Vol 33 (2) ◽  
pp. 142-151 ◽  
Author(s):  
Orsola Tiboni ◽  
Rita Cantoni ◽  
Roberta Creti ◽  
Piero Cammarano ◽  
Anna Maria Sanangelantoni
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Elongation Factor ◽  
Elongation Factor G ◽  
Str Operon ◽  
Factor G

Molecular characterization, expression analysis and RNAi knock-down of elongation factor 1α and 1γ from Nilaparvata lugens and its yeast-like symbiont

2016 ◽  
Vol 107 (3) ◽  
pp. 303-312 ◽  
Author(s):  
W.X. Wang ◽  
T.H. Zhu ◽  
K.L. Li ◽  
L.F. Chen ◽  
F.X. Lai ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Sequence Homology ◽  
Fat Body ◽  
Quantitative Polymerase Chain Reaction ◽  
Elongation Factor ◽  
Nilaparvata Lugens ◽  
Expression Level ◽  
Amino Acid Sequence Homology ◽  
Qpcr Analysis

AbstractIn the present paper, four cDNAs encoding the alpha and gamma subunits of elongation factor 1 (EF-1) were cloned and sequenced from Nilaparvata lugens, named NlEF-1α, NlEF-1γ, and its yeast-like symbiont (YLS), named YsEF-1α and YsEF-1γ, respectively. Comparisons with sequences from other species indicated a greater conservation for EF-1α than for EF-1γ. NlEF-1α has two identical copies. The deduced amino acid sequence homology of NlEF-1α and NlEF-1γ is 96 and 64%, respectively, compared with Homalodisca vitripennis and Locusta migratoria. The deduced amino acid sequence homology of YsEF-1α and YsEF-1γ is 96 and 74%, respectively, compared with Metarhizium anisopliae and Ophiocordyceps sinensis. Reverse transcription-quantitative polymerase chain reaction (RT–qPCR) analysis revealed that the expression level of NlEF-1α and NlEF-1γ mRNA in hemolymph, ovary, fat body and salivary glands were higher than the midgut and leg tissue. YsEF-1α and YsEF-1γ was highly expressed in fat body. The expression level of NlEF-1α was higher than that of NlEF-1γ. Through RNA interference (RNAi) of the two genes, the mortality of nymph reached 92.2% at the 11th day after treatment and the ovarian development was severely hindered. The RT–qPCR analysis verified the correlation between mortality, sterility and the down-regulation of the target genes. The expression and synthesis of vitellogenin (Vg) protein in insects injected with NlEF-1α and NlEF-1γ double-stranded RNA (dsRNA) was significantly lower than control groups. Attempts to knockdown the YsEF-1 genes in the YLS was unsuccessful. However, the phenotype of N. lugens injected with YsEF-1α dsRNA was the same as that injected with NlEF-1α dsRNA, possibly due to the high similarity (up to 71.9%) in the nucleotide sequences between NlEF-1α and YsEF-1α. We demonstrated that partial silencing of NlEF-1α and NlEF-1γ genes caused lethal and sterility effect on N. lugens. NlEF-1γ shares low identity with that of other insects and therefore it could be a potential target for RNAi-based pest management.

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