Hostname: page-component-586b7cd67f-rdxmf Total loading time: 0 Render date: 2024-11-27T19:33:54.557Z Has data issue: false hasContentIssue false

A hierarchy of RNA subdomains in assembly of the central domain of the 30 S ribosomal subunit

Published online by Cambridge University Press:  01 March 2000

SULTAN C. AGALAROV
Affiliation:
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA Institute for Protein Research, Russian Academy of Sciences, Pushchino, Russia
JAMES R. WILLIAMSON
Affiliation:
Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA
Get access

Abstract

Beginning with the framework that has been developed for the assembly of the 30 S ribosomal subunit, we have identified a series of RNAs that are minimal binding sites for proteins S15, S6, S18, and S11 in the central domain from Thermus thermophilus. The minimal binding RNA for proteins S15, S6, and S18 consists of helix 22 and three-way junctions at both ends composed of portions of helices 20, 21, and 23. Addition of the remaining portion of helix 23 to this construct results in the minimal site for S11. Surprisingly, almost half of the central domain (helices 24, 25, and 26) is dispensable for binding the central domain proteins. Thus, at least two classes of RNA elements can be identified in ribosomal RNA. A protein-binding core element (such as helices 20, 21, 22, and 23) is required for the association of ribosomal proteins, whereas secondary binding elements (such as helices 24, 25, and 26) associate only with the preformed core RNP complex. Apparently, there may be a hierarchy of ribosomal RNA elements similar to the hierarchy of primary, secondary, and tertiary binding ribosomal proteins.

Type
Research Article
Copyright
2000 RNA Society

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)