Size and shape of isolated proteins of the small ribosomal subunit of rat liver

Behlke, Joachim; Theise, H; F, Noll; Bielka, H

doi:10.1016/0014-5793(79)80732-2

Cited by 4 publications

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References 17 publications

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“…The different electrophoretic systems used are listed in Table I. proteins S3, S3a and S13 are located in the 'head' of the particle adjacent to the cleft between 'head' and 'body'. The elongated protein S6 (Behlke et al, 1979) has been mapped by immune electron microscopy (Lutsch et al, in preparation) to occur at the site indicated in the model and in a second position (not shown) near to the cleft but on the 'body' of the subunit. Experiments involving affinity labelling and cross-linking have revealed that proteins S3, S3a and S6 are involved in interactions with poly(U) [Stahl and Kobets, 1981 (S3, S3a); Terao and Ogata, 1979 (S6)] and natural mRNA [Takahashi and Ogata, 1981 (S3a, S6)].…”

Section: Discussionmentioning

confidence: 99%

Spatial arrangement of proteins within the small subunit of rat liver ribosomes studied by cross-linking.

1983

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Cross-linking of proteins within the small subunit of rat liver ribosomes by the bifunctional reagent dimethyl 4,7-dioxo-5,6-dihydroxy-3,8-diazadecanbisimidate produced numerous covalently linked protein dimers which could be separated by a combination of ion-exchange chromatography on carboxymethyl cellulose and polyacrylamide gel electrophoresis. The protein components of the dimers were identified electrophoretically after periodate cleavage of the cross-link(s). The analysis revealed 42 cross-linked dimers involving 25 different proteins. Among these, proteins S3, S4 and S20 occurred in combinations with six, eight and seven different proteins, respectively. For proteins S13, S14 and S17 five protein neighbours could be identified, while 13 of the remaining proteins were linked to three or four different protein partners. The involvement of the majority of proteins in the formation of multiple cross-linked dimers implies that a large number of protein-protein interaction sites exist within the ribosomal subunit. A preliminary model illustrating the arrangement of 16 proteins in the small ribosomal subunit is presented and discussed with respect to possible functions, especially in the event of translation initiation.

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Section: Discussionmentioning

confidence: 99%