Crosslinking of initiation factor eIF‐2 to proteins of the small subunit of rat liver ribosomes

Westermann, Peter; Heumann, W.; Bommer, Ulrich‐Axel; Bielka, H; Nygård, Odd; Hultin, T.

doi:10.1016/0014-5793(79)80061-7

Cited by 85 publications

(42 citation statements)

References 13 publications

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“…The results of the experiments indicated that eIF-2 interacts with ribosomal proteins $3, S3a, $6, S13/16, S19 and $24. (The nomenclature of ribosomal proteins used in this paper follows that of McConkey et al [14], whereas in [1,3] an earlier nomenclature was applied [15].) This is in agreement with the results of our antibody inhibition experiments, with the exception of protein $3.…”

Section: Resultssupporting

confidence: 85%

“…But our earlier conclusion that protein $6 participates in eIF-2 binding [4] is supported by crosslinking experiments [1,2]. The location of the respective ribosomal proteins on the surface of the 40 S subunit as demonstrated by immunoelectron microscopy [6][7][8] together with the recently observed eIF-2-binding area [9] are shown in a schematic drawing in fig.3.…”

Section: Resultsmentioning

confidence: 88%

“…Another approach to investigate the interaction between 40 S ribosomal proteins and initiation factor eIF-2 was chemical crosslinking [1,2]. The results of the experiments indicated that eIF-2 interacts with ribosomal proteins $3, S3a, $6, S13/16, S19 and $24.…”

Section: Resultsmentioning

confidence: 99%

“…This is in agreement with the results of our antibody inhibition experiments, with the exception of protein $3. The observed crosslinking of protein $3 to eIF-2 [1] could be explained by indirect crosslinking via protein S3a, because in all crosslinking studies with 40 S ribosomal subunits proteins $3 and S3a were identified as neighboured proteins (for review see [51). eIF-2 Fig.3.…”

Section: Resultsmentioning

confidence: 99%

“…The interaction of proteins of the 40 S ribosomal subunit with initiation factor elF-2 in the quaternary initiation complex [elF-2 × GTP x Met-tRNAf x 40 S subunit] has been investigated by crosslinking experiments [1,2] as well as by application of antibodies against ribosomal proteins [3,4] (review [5]). Most of the proteins shown to be involved in elF-2 binding have been located at the surface of the 40 S ribosomal subunit by immunoelectron microscopy [6][7][8].…”

Section: Introductionmentioning

confidence: 99%

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Identification of proteins of the 40 S ribosomal subunit involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex by means of monospecific antibodies

et al. 1988

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Monospecific polyclonal antibodies against seven proteins of the 40 S subunit of rat liver ribosomes were used to identify ribosomal proteins involved in interaction with initiation factor elF-2 in the quaternary initiation complex [elF-2 x GMPPCP x [aH]Met-tRNAf x 40 S ribosomal subunit]. Dimeric immune complexes of 40 S subunits mediated by antibodies against ribosomal proteins S3a, S13/16, S19 and $24 were found to be unable to bind the ternary initiation complex [elF-2 x GMPPCP x pH]Met-tRNAf]. In contrast, 40 S dimers mediated by antibodies against proteins $2, $3 and S 17 were found to bind the ternary complex. Therefore, from the ribosomal proteins tested, only proteins S3a, S 13/ 16, S!9 and $24 are concluded to be involved in elF-2 binding to the 40 S subunit.40 S ribosomal subunit; elF-2 binding; Inhibitory antibody; Ribosomal protein

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Section: Resultssupporting

confidence: 85%

Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Identification of proteins of the 40 S ribosomal subunit involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex by means of monospecific antibodies

et al. 1988

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Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry

Martínek

Mozhaev

1985

Advances in Enzymology - And Related Areas of Molecular Biology

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Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes.

Nygård¹,

Nika²

1982

The EMBO Journal

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Protein constituents at the subunit interface of rat liver ribosomes were analysed by cross‐linking with the bifunctional reagent, diepoxybutane (distance between reactive groups 4 A). Isolated 40S and 60S subunits were labelled with 125I and recombined with unlabelled complementary subunits. The two kinds of selectively labelled 80S ribosomes were treated with diepoxybutane at low concentration. Radioactive ribosomal proteins covalently attached to the rRNA of the unlabelled complementary subparticles were isolated by repeated gradient centrifugation. The RNA‐bound, labelled proteins were identified by two‐dimensional gel electrophoresis. The experiments showed that proteins S2, S3, S4, S6, S7, S13, and S14 in the small subunit of rat liver ribosomes are located at the ribosomal interface in close proximity to 28S rRNA. Similarly, proteins L3, L6, L7, and L8 were found at the the interface of the large ribosomal subunit in the close vicinity of 18S rRNA.

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Crosslinking of initiation factor eIF‐2 to proteins of the small subunit of rat liver ribosomes

Cited by 85 publications

References 13 publications

Identification of proteins of the 40 S ribosomal subunit involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex by means of monospecific antibodies

Identification of proteins of the 40 S ribosomal subunit involved in interaction with initiation factor eIF‐2 in the quaternary initiation complex by means of monospecific antibodies

Immobilization of Enzymes: An Approach to Fundamental Studies in Biochemistry

Identification by RNA-protein cross-linking of ribosomal proteins located at the interface between the small and the large subunits of mammalian ribosomes.

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