Byasmuni, ; Burma, D. P. (1982) Structural alteration of rRNA in the L7/L12 region of 50S ribosome on removal of L7/L12 proteins Biochemical and Biophysical Research Communications, 104 (1). pp. 99-104. ISSN 0006-291X
Full text not available from this repository.
Official URL: http://linkinghub.elsevier.com/retrieve/pii/000629...
Related URL: http://dx.doi.org/10.1016/0006-291X(82)91945-3
Core particles of 50S ribosomes depleted of L7/L12 proteins are degraded by RNase I at a considerably slower rate than intact 50S ribosomes. The normal rate is restored on incorporating L7/L12 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 L7/L12 proteins has less ordered structure which, on removal of L7/L12 proteins, becomes more organized. Apparently, binding of L7/L12 proteins to the 50S core leads to the destabilization of double-stranded regions of rRNA.
|Source:||Copyright of this article belongs to Elsevier Science.|
|Deposited On:||06 Dec 2010 18:13|
|Last Modified:||28 May 2011 10:05|
Repository Staff Only: item control page