Structural alteration of rRNA in the L7/L12 region of 50s ribosome on removal of L7/L12 proteins |
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Authors: | Burma" target="_blank">D P ByasmuniBurma |
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Institution: | Molecular Biology Unit, Department of Biochemistry, Institute of Medical Sciences, Banaras Hindu University, Varanasi-221005, U.P., India |
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Abstract: | Core particles of 50S ribosomes depleted of proteins are degraded by RNase I at a considerably slower rate than intact 50S ribosomes. The normal rate is restored on incorporating proteins into the core particles. The capacity of the core particles to inhibit the RNase I-catalyzed hydrolysis of poly A and to bind ethidium bromide is also greater with core particles than with intact 50S ribosomes. It appears from these results that the region(s) of rRNA in the vicinity of proteins has less ordered structure which, on removal of proteins, becomes more organized. Apparently, binding of proteins to the 50S core leads to the destabilization of double-stranded regions of rRNA. |
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