Polypeptide elongation factor 1 and the control of elongation rate in rat liver in vivo

Nature ◽  
1976 ◽  
Vol 264 (5588) ◽  
pp. 804-806 ◽  
Author(s):  
JENNIFER B. K. NIELSEN ◽  
PATRICIA W. PLANT ◽  
AUDREY E. V. HASCHEMEYER
Keyword(s):  
Rat Liver ◽  
Elongation Factor ◽  
Elongation Rate ◽  
Elongation Factor 1

scholarly journals Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends.

1996 ◽  
Vol 135 (5) ◽  
pp. 1309-1321 ◽  
Author(s):  
J W Murray ◽  
B T Edmonds ◽  
G Liu ◽  
J Condeelis
Keyword(s):  
Actin Filaments ◽  
Actin Polymerization ◽  
Elongation Factor ◽  
Protein Translation ◽  
Binding Activity ◽  
Dependent Manner ◽  
Molar Ratios ◽  
Elongation Factor 1 Alpha ◽  
Elongation Factor 1

Elongation factor 1 alpha (EF1 alpha) is an abundant protein that binds aminoacyl-tRNA and ribosomes in a GTP-dependent manner. EF1 alpha also interacts with the cytoskeleton by binding and bundling actin filaments and microtubules. In this report, the effect of purified EF1 alpha on actin polymerization and depolymerization is examined. At molar ratios present in the cytosol, EF1 alpha significantly blocks both polymerization and depolymerization of actin filaments and increases the final extent of actin polymer, while at high molar ratios to actin, EF1 alpha nucleates actin polymerization. Although EF1 alpha binds actin monomer, this monomer-binding activity does not explain the effects of EF1 alpha on actin polymerization at physiological molar ratios. The mechanism for the inhibition of polymerization is related to the actin-bundling activity of EF1 alpha. Both ends of the actin filament are inhibited for polymerization and both bundling and the inhibition of actin polymerization are affected by pH within the same physiological range; at high pH both bundling and the inhibition of actin polymerization are reduced. Additionally, it is seen that the binding of aminoacyl-tRNA to EF1 alpha releases EF1 alpha's inhibiting effect on actin polymerization. These data demonstrate that EF1 alpha can alter the assembly of F-actin, a filamentous scaffold on which non-membrane-associated protein translation may be occurring in vivo.

scholarly journals In vivo characterization of the role of tissue‐specific translation elongation factor 1 A 2 in protein synthesis reveals insights into muscle atrophy

FEBS Journal ◽  
2013 ◽  
Vol 280 (24) ◽  
pp. 6528-6540 ◽  
Author(s):  
Jennifer Doig ◽  
Lowri A. Griffiths ◽  
David Peberdy ◽  
Permphan Dharmasaroja ◽  
Maria Vera ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Atrophy ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
In Vivo Characterization ◽  
Elongation Factor 1

scholarly journals Growth of liver accompanied by an increased binding of aminoacyl-transfer ribonucleic acids

1977 ◽  
Vol 166 (3) ◽  
pp. 463-471 ◽  
Author(s):  
D McEwen Nicholls ◽  
J Carey ◽  
W Sendecki
Keyword(s):  
Rat Liver ◽  
Inhibitory Activity ◽  
Elongation Factor ◽  
Supernatant Fraction ◽  
Regenerating Liver ◽  
Ribosomal Subunits ◽  
Ribonucleic Acids ◽  
Aminoacyl Transfer ◽  
Elongation Factor 1 ◽  
Trna Binding

Homogenates of rat liver obtained 3 or 14 days after partial hepatectomy were used to prepare the postmicrosomal pH5-supernatant fraction and to prepare salt-wash fractions of the 40S ribosomal subunits and the 80S ribosomes. The factor-dependent binding of methionyl-tRNAfMet to ribosomes and the elongation-factor-1-dependent binding of phenylalanyl-tRNA to ribosomes were both increased after 3 days of growth, but not after 14 days of growth. An activity inhibitory to phenylalanyl-tRNA binding that was located in ribosomal wash fractions was decreased after 14 days of growth. Since the decreased inhibitory activity was obtained from the ribosomes and was tested against ribosomes and excess of pH5-supernatant fraction from control rat liver, its action was separate from the phenylalanyl-tRNA binding activities of the pH5-supernatant fractions from sham-operated and regenerating liver.

Multiple forms and some properties of aminoacyltransferase I (elongation factor 1) from rat liver

Biochemistry ◽  
1972 ◽  
Vol 11 (22) ◽  
pp. 4187-4194 ◽  
Author(s):  
James F. Collins ◽  
Hong Mo Moon ◽  
Elizabeth S. Maxwell
Keyword(s):  
Rat Liver ◽  
Elongation Factor ◽  
Multiple Forms ◽  
Elongation Factor 1

scholarly journals Characterization of Diaporthe species associated with peach constriction canker, with two novel species from China

MycoKeys ◽  
2021 ◽  
Vol 80 ◽  
pp. 77-90
Author(s):  
Xianhong Wang ◽  
Yashuang Guo ◽  
Yamin Du ◽  
Ziling Yang ◽  
Xinzhong Huang ◽  
...  
Keyword(s):  
Internal Transcribed Spacer ◽  
Novel Species ◽  
Phylogenetic Analyses ◽  
Elongation Factor ◽  
Translation Elongation Factor ◽  
Translation Elongation ◽  
Wide Range ◽  
Elongation Factor 1

Species of Diaporthe infect a wide range of plants and live in vivo as endophytes, saprobes or pathogens. However, those in peach plants are poorly characterized. In this study, 52 Diaporthe strains were isolated from peach branches with buds, showing constriction canker symptoms. Phylogenetic analyses were conducted using five gene regions: internal transcribed spacer of the ribosomal DNA (ITS), translation elongation factor 1-α (TEF), ß-tubulin (TUB), histone (HIS), and calmodulin (CAL). These results coupled with morphology revealed seven species of Diaporthe, including five known species (D. caryae, D. cercidis, D. eres, D. hongkongensis, and D. unshiuensis). In addition, two novel species D. jinxiu and D. zaofenghuang are introduced. Except for the previously reported D. eres, this study represents the first characterization of Diaporthe species associated with peach constriction canker in China, and contributes useful data for practicable disease management.

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