UZH-Logo

Maintenance Infos

Multiple roles of metal ions in large ribozymes


Donghi, D; Schnabl, J (2011). Multiple roles of metal ions in large ribozymes. In: Sigel, Astrid; Sigel, Helmut; Sigel, Roland K O. Structural and Catalytic Roles of Metal Ions in RNA. Cambridge, UK: Royal Society of Chemistry, 197-234.

Abstract

Since the discovery of catalytic RNA molecules (ribozymes), intense research has been devoted to understand their structure and activity. Among RNA molecules, the large ribozymes, namely group I and group II introns and RNase P, are of special importance. The first two ribozymes are known for their ability to perform self-splicing while RNase P is responsible for the 5'-end maturation of tRNA in bacteria, archea, and eukaryotes. All three groups of ribozymes show a significant requirement for metal ions in order to establish the active tertiary structure that enables catalysis. The primary role of both monovalent and divalent metal ions is to screen the negative charge associated with the phosphate sugar backbone, but the metal ions also play an active role in catalysis. Biochemical and biophysical investigations, supported by recent findings from X-ray crystal structures, allow clarifying and rationalizing both the structural and catalytic roles of metal ions in large ribozymes. In particular, the "two-metal-ion mechanism", describing how metal ions in the active center take part in catalysis, has been largely corroborated.

Abstract

Since the discovery of catalytic RNA molecules (ribozymes), intense research has been devoted to understand their structure and activity. Among RNA molecules, the large ribozymes, namely group I and group II introns and RNase P, are of special importance. The first two ribozymes are known for their ability to perform self-splicing while RNase P is responsible for the 5'-end maturation of tRNA in bacteria, archea, and eukaryotes. All three groups of ribozymes show a significant requirement for metal ions in order to establish the active tertiary structure that enables catalysis. The primary role of both monovalent and divalent metal ions is to screen the negative charge associated with the phosphate sugar backbone, but the metal ions also play an active role in catalysis. Biochemical and biophysical investigations, supported by recent findings from X-ray crystal structures, allow clarifying and rationalizing both the structural and catalytic roles of metal ions in large ribozymes. In particular, the "two-metal-ion mechanism", describing how metal ions in the active center take part in catalysis, has been largely corroborated.

Citations

12 citations in Web of Science®
13 citations in Scopus®
Google Scholar™

Altmetrics

Additional indexing

Item Type:Book Section, refereed, further contribution
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Language:English
Date:2011
Deposited On:29 Mar 2012 09:01
Last Modified:30 Oct 2016 06:17
Publisher:Royal Society of Chemistry
Series Name:Metal Ions in Life Sciences
Number:9
ISSN:1559-0836
ISBN:978-1-84973-094-5
Publisher DOI:https://doi.org/10.1039/978184973251200197
Related URLs:http://www.rsc.org/shop/books/2011/9781849730945.asp (Publisher)
http://www.recherche-portal.ch/ZAD:default_scope:ebi01_prod006495315 (Library Catalogue)
PubMed ID:22010273

Download

Full text not available from this repository.
View at publisher

TrendTerms

TrendTerms displays relevant terms of the abstract of this publication and related documents on a map. The terms and their relations were extracted from ZORA using word statistics. Their timelines are taken from ZORA as well. The bubble size of a term is proportional to the number of documents where the term occurs. Red, orange, yellow and green colors are used for terms that occur in the current document; red indicates high interlinkedness of a term with other terms, orange, yellow and green decreasing interlinkedness. Blue is used for terms that have a relation with the terms in this document, but occur in other documents.
You can navigate and zoom the map. Mouse-hovering a term displays its timeline, clicking it yields the associated documents.

Author Collaborations