Interaction of polypeptide chain elongation factors with rat liver ribosomal subunits

Rao, P. Nageswara; Moldave, Kivie

doi:10.1016/0022-2836(69)90188-0

Cited by 39 publications

(14 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Relative to the 40S subunit, little or no binding was detected for 60S subunits with phenylalanyl-tRNA. In general the requirements for enzymatic binding of aminoacyl-tRNA to pea 40S subunits are similar to those reported for mammalian 40S subunits (8,21) and bacterial 30S subunits (14). The low level of binding of aminoacyl-tRNA to the small subparticles observed here in the absence of supernatant enzyme is similar to that which has been reported for both procaryote and eucaryote ribosomes (4, 9, 19).…”

Section: Resultssupporting

confidence: 88%

See 1 more Smart Citation

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Lin

Key

1971

Plant Physiol.

View full text Add to dashboard Cite

The dissociation of N2 gas-induced monomeric ribosomes from the pea root was studied by varying the concentration of KCI (or NILCI) and MgCL2 in the presence of dithiothreitoL These monoribosomes were shown to dissociate completely into subunits at 0.5 M KCI or NH4CI in the presence of 5 mM MgCI2. The 40S subunits were more susceptible to structural change in KC1 than were the 60S subunits. On the other hand, the 60S subunits appeared to be more labile to NH4CI.The activity of the subunits relative to aminoacyl-tRNA binding and peptide bond formation was investigated using subunits derived from 0.5 M KCI (or NH4CI)

show abstract

Section: Resultssupporting

confidence: 88%

“…Numerous workers (11,13,18,21,22) ide gel electrophoresis of the RNA extracted from the subunits and also by recentrifugation of the subunits separately on sucrose gradients containing tris buffer. Preparation of Aminoacyl-tRNA Binding and Transfer Enzymes.…”

mentioning

confidence: 99%

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Lin

Key

1971

Plant Physiol.

View full text Add to dashboard Cite

show abstract

“…that the action of the translocation factor in mammalian system may be localized on the larger ribosomal subunit, as has been reported for E. coli [6,7] . Rao and Moldave [3] have studied binding of transferase II to ribosomal subunits from salt-washed ribosomes in a rat liver system, and have reported finding significant binding only in the presence of both ribosomal subunits. The differences in conditions of incubation and centrifugation may account for the difference observed.…”

Section: Resultsmentioning

confidence: 99%

“…Transferase I has been shown to function in the binding of aminoacyl-tRNA to ribosomes [ 1,2] , and evidence has been reported that transferase I (or a complex containing it) interacts specifically with the 40 S ribosomal subunit [3]. Transferase II has been demonstrated to function in translocation of peptidyl-tRNA from the acceptor to the donor site on ribosomes [2,4,5] , but the exact location of its action is not known.…”

Section: Introductionmentioning

confidence: 99%

Interaction of transferase II with the 60 s ribosomal subunit

Traugh

Collier

1971

FEBS Letters

View full text Add to dashboard Cite

“…Smulson and Rideau [24] also could not detect a binding of EF-2 to ribosomal subunits. Rao and Moldave [25] reported that rat liver 40-S subunits are capable of interacting with EF-1 in the presence of aminoacyl-tRNA and poly(uridy1ic acid) ; a guanosine nucleotide was not required for this interaction. Their EF-1, however, was impure.…”

Section: Discussionmentioning

confidence: 98%

The Binding of Tritiated Elongation Factors 1 and 2 to Ribosomes from Krebs II Mouse Ascites Tumor Cells

Nolan

Grasmuk

Drews

1975

European Journal of Biochemistry

View full text Add to dashboard Cite

Tritiated elongation factors 1 and 2 (EF-1 and EF-2) were obtained from Krebs I1 ascites cells which had been grown in mice injected with radioactive amino acids. The highly purified factors were sufficiently radioactive to be used in a study of the interactions between ribosomes and elongation factors.The following results were obtained. 1. EF-1 binding to ribosomes requires the presence of a polynucleotide, an aminoacyl-tRNA specified by the latter and a guanosine nucleotide carrying three phosphate groups. The hydrolysis of the GTP molecule involved in the binding reaction leads to the immediate release of EF-1. If GTP is replaced by Guo-5'-P,-CH2-P the factor remains bound to the ribosome and can be detected by sucrose gradient centrifugation techniques.2. Likewise EF-2 binding to ribosomes can only be detected in the presence of Guo-5'-P2-CH2-P. 3. The affinity of ribosomes for EF-2 appears to be higher than for EF-1: preincubation of ribosomes with EF-2 inhibits the subsequent attachment of EF-1 almost completely. EF-1 prebound to ribosomes in the presence of Guo-5'-P2-CH2-P, poly(uridy1ic acid) and Phe-tRNAPhe is partially removed from the ribosomes together with Phe-tRNA during a second incubation with EF-2.4. Although EF-2 binding to ribosomes precludes any stable association between ribosomes and EF-1 it does not prevent the insertion of aminoacyl-tRNA into the ribosomal A-site. The attachment of aminoacyl-tRNA under these conditions enhances the binding of EF-2 to the ribosome.5. The antibiotic showdomycin strongly inhibits the attachment of EF-1 to ribosomes and to a lesser degree impairs the binding of EF-2.6. A-site ribosomes display a strong preference for the attachment of EF-2 and bind EF-1 only very poorly. The reverse is true for P-site ribosomes which are good substrates for the binding of EF-1 and bind EF-2 less efficiently than A-site ribosomes.These results and a number of additional findings made in this and in previous studies are discussed in the general context of the structure and function of mammalian elongation factors 1 and 2.Elongation factor 1 (EF-1) from ascites tumor cells occurs in multiple forms. All of these appear to be composed of aggregates of different numbers of a single polypeptide chain with an approximate molecular weight of 47000 [l]. The pure tetramer form of EF-1 was shown to carry one binding site for guanosine nucleotides which can be occupied by GTP, GDP or Guo-S-P,-CH,-P [2]. The binding constants of EF-1 for both GDP and GTP appear to be approximately lo5 M-' but only the binding of GTP conveyedAbbreviations. EF-1, elongation factor 1 ; EF-2, elongation factor 2; Guo-5'-P2-CH2-P, 5'-guanylyl-methylene-diphosphonate.to elongation factor 1 the capacity to specifically interact with the aminoacyl-tRNA [2]. The fact that Guo-5'-CH2-P could promote the EF-I-directed binding of aminoacyl-tRNA to ribosomes [3], while only promoting slight aminoacyl-tRNA protection against deacylation in an EF-1-dependent protection assay [2], indicated that these two functions of th...

show abstract

Interaction of polypeptide chain elongation factors with rat liver ribosomal subunits

Cited by 39 publications

References 31 publications

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Interaction of transferase II with the 60 s ribosomal subunit

The Binding of Tritiated Elongation Factors 1 and 2 to Ribosomes from Krebs II Mouse Ascites Tumor Cells

Contact Info

Product

Resources

About

Interaction of polypeptide chain elongation factors with rat liver ribosomal subunits

Cited by 39 publications

References 31 publications

Dissociation of N2 Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Dissociation of N2 Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Interaction of transferase II with the 60 s ribosomal subunit

The Binding of Tritiated Elongation Factors 1 and 2 to Ribosomes from Krebs II Mouse Ascites Tumor Cells

Contact Info

Product

Resources

About

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea

Dissociation of N₂ Gas-induced Monomeric Ribosomes and Functioning of the Derived Subunits in Protein Synthesis in Pea