[Mutual effect of human ribosomal proteins S5 and S16 on their binding with 18S rRNA fragment 1203-1236/1521-1698].
Human ribosomal proteins S5 and S16 are homologues of prokaryotic ribosomal proteins S7p and S9p, respectively, that according to X-ray crystallography data on the Thermus thermophilus 30S ribosomal subunit contact the 3'-terminal 16S rRNA region formed by helices H28-H30 and H38-H43. In the present work we report studying mutual effect of human ribosomal proteins S5 and S16 on their binding with RNA transcript corresponding to the region 1203-1236/1521-1698 of the 18S rRNA (helices H28-30 and H41-43), which is homologous to thel6S rRNA region known to contain binding site of S7p and part of binding site of S9p. It was shown that simultaneous binding of ribosomal proteins S5 and S16 with this RNA transcript causes conformational changes in it stabilizing the complex by involvement of new parts of the RNA that interact with neither S5 nor S16 in the respective binary complexes.
Ian'shina
D D
DD
Malygin
A A
AA
Karpova
G G
GG
D006801:Humans; D011485:Protein Binding / Q000502:physiology; D012336:RNA, Ribosomal, 16S / Q000737:chemistry / Q000378:metabolism; D012337:RNA, Ribosomal, 18S / Q000737:chemistry* / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism; D054680:Ribosome Subunits, Small, Bacterial / Q000737:chemistry / Q000378:metabolism; D016963:Thermus thermophilus / Q000737:chemistry / Q000378:metabolism
D012336:RNA, Ribosomal, 16S; D012337:RNA, Ribosomal, 18S; D012269:Ribosomal Proteins; C421090:Rps16 protein, human; C030831:ribosomal protein S5