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Affinity modification of the 40S subparticle from human placenta with derivatives of pAUG and pAUGU3

Mundus, D.A.; Malygin, A.A.; Zenkova, M.A.; Repkova, M.N.; Ven'iaminova, A.G.; Smailov, S.K.; Li, A.V.; Iskakov, B.K.; Vratskikh, L.V.; Iamkovoĭ, V.I.

Molekuliarnaia Biologiia 26(4): 949-956

1992

ISSN/ISBN: 0026-8984
PMID: 1435786
Document Number: 391010
Affinity labeling of 40S subunits from human placenta with 4-(N-2-chloroethyl-N-methylamino)benzylmethyl-[32P]phosphoamide s of oligoribonucleotides pAUG and pAUGU3 was studied. Covalent attachment of these derivatives to 40S subunits within the complexes with 40S subunits, formed in the presence of Met-tRNAf.eIF-2.GTP, was detected. Both rRNA and ribosomal proteins were modified. Fragments of 18S rRNA, containing sites of the reagent attachment were identified: 1058-1164 for pAUG derivative and 976-1057--for pAUG and pAUGU3 ones. The data obtained allowed to conclude that the presence of the neighbouring codon at the A-site, regardless of the presence of the tRNA in it, affects significantly the arrangement of the trinucleotide template in the codon-anticodon interaction region. The large subunit does not cause significant alterations in the structural organization of the codon-anticodon interaction region.

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