Ribozymes, the first 20 years

2002 ◽  
Vol 30 (6) ◽  
pp. 1162-1166 ◽  
Author(s):  
T. R. Cech
Keyword(s):  
In Vitro Selection ◽  
Tertiary Structure ◽  
Catalytic Rna ◽  
Rna Catalysis ◽  
X Ray Crystallography ◽  
Mechanistic Analysis ◽  
Self Splicing ◽  
Secondary And Tertiary Structure

In 1982 we reported the first catalytic RNA or ribozyme: the self-splicing intron of the Tetrahymena pre-rRNA. Additional examples of natural ribozymes were soon found, and research in the field focused on their enzymic mechanism and secondary and tertiary structure. Ribozymes identified through in vitro selection extended the repertoire of RNA catalysis. Two directions of current and future interest are the determination of atomic-resolution structures of large ribozymes by X-ray crystallography and the structural and mechanistic analysis of complexes of ribozymes with protein facilitators of their activity.

Quantitative determination of the number of secondary and tertiary structure base pairs in transfer RNA in solution

Biochemistry ◽  
1976 ◽  
Vol 15 (20) ◽  
pp. 4370-4377 ◽  
Author(s):  
P. H. Bolton ◽  
C. R. Jones ◽  
D. Bastedo-Lerner ◽  
K. L. Wong ◽  
D. R. Kearns
Keyword(s):  
Quantitative Determination ◽  
Tertiary Structure ◽  
Transfer Rna ◽  
Base Pairs ◽  
Secondary And Tertiary Structure

scholarly journals Interaction of Quillaja bark saponin and bovine serum albumin: Effect on secondary and tertiary structure, gelation and in vitro digestibility of the protein

LWT ◽  
2020 ◽  
Vol 121 ◽  
pp. 108970 ◽  
Author(s):  
Elaine Kaspchak ◽  
Cíntia Tiemi Misugi Kayukawa ◽  
Joana Léa Meira Silveira ◽  
Luciana Igarashi-Mafra ◽  
Marcos R. Mafra
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Tertiary Structure ◽  
In Vitro Digestibility ◽  
Secondary And Tertiary Structure

Synthesis of Pyrophosphates for In Vitro Selection of Catalytic RNA Molecules

2008 ◽  
Vol 27 (1) ◽  
pp. 43-56 ◽  
Author(s):  
Hyo-Joong Kim ◽  
Myong Jung Kim ◽  
Nilesh Karalkar ◽  
Daniel Hutter ◽  
Steven A. Benner
Keyword(s):  
In Vitro Selection ◽  
Catalytic Rna ◽  
Rna Molecules ◽  
Selection Of

In vitro selection of hemin-binding catalytic RNA

2009 ◽  
Vol 19 (5) ◽  
pp. 1484-1487 ◽  
Author(s):  
Mingzhe Liu ◽  
Takuma Kagahara ◽  
Hiroshi Abe ◽  
Yoshihiro Ito
Keyword(s):  
In Vitro Selection ◽  
Catalytic Rna ◽  
Selection Of

scholarly journals Functional Profiling and Crystal Structures of Isothiocyanate Hydrolases Found in Gut-Associated and Plant-Pathogenic Bacteria

2018 ◽  
Vol 84 (14) ◽  
Author(s):  
Tijs J. M. van den Bosch ◽  
Kemin Tan ◽  
Andrzej Joachimiak ◽  
Cornelia U. Welte
Keyword(s):  
Active Site ◽  
Pathogenic Bacteria ◽  
Tertiary Structure ◽  
Crop Protection ◽  
X Ray Crystallography ◽  
Beneficial Effects ◽  
Functional Profiling ◽  
Cruciferous Plants

ABSTRACT Isothiocyanates (ITCs) are produced by cruciferous plants to protect them against herbivores and infection by microbes. These compounds are of particular interest due to their antimicrobial and anticarcinogenic properties. The breakdown of ITCs in nature is catalyzed by isothiocyanate hydrolases (ITCases), a novel family within the metallo-β-lactamase (MBL)-fold superfamily of proteins. saxA genes that code for ITCases are particularly widespread in insect- and plant-associated bacteria. Enzymatic characterization of seven phylogenetically related but distinct ITCases revealed similar activities on six selected ITCs, suggesting that phylogenetic diversity does not determine the substrate specificity of ITCases. X-ray crystallography studies of two ITCases sharing 42% amino acid sequence identity revealed a highly conserved tertiary structure. Notable features of ITCases include a hydrophobic active site with two Zn 2+ ions coordinating water/hydroxide and a flexible cap that is implicated in substrate recognition and covers the active site. This report reveals the function and structure of the previously uncharacterized family of isothiocyanate hydrolases within the otherwise relatively well-studied superfamily of metallo-β-lactamases. IMPORTANCE This study explores a newly discovered protein in the β-lactamase superfamily, namely, SaxA, or isothiocyanate hydrolase. Isothiocyanates are defensive compounds found in many cabbage-related crop plants and are currently being investigated for their antimicrobial and anticarcinogenic properties. We show that isothiocyanate hydrolases are responsible for the breakdown of several of these plant defensive chemicals in vitro and suggest their potential for mitigating the beneficial effects of isothiocyanates in crop protection and cancer prevention.

Mithochondrial biogenesis: recent developments and insights

1988 ◽  
Vol 319 (1193) ◽  
pp. 85-95
Keyword(s):  
Rna Splicing ◽  
Mitochondrial Genes ◽  
Pivotal Role ◽  
Mitochondrial Proteins ◽  
Rna Catalysis ◽  
Expression Of Genes ◽  
Recent Developments ◽  
Self Splicing ◽  
Shed Light

Biosynthesis of a functional mitochondrion requires the coordinate expression of genes in both mitochondrial and nuclear DNAs. In yeast, three mitochondrial genes are split and RNA splicing plays a pivotal role in their expression. The recent finding that some introns are capable of self-splicing activity in vitro has permitted analysis of the mechanisms involved in RNA catalysis and may eventually shed light on the evolution of splicing mechanisms in general. Most mitochondrial proteins are encoded by nuclear genes, synthesized in the cytoplasm and imported by the organelle. The availability of cloned genes coding for several constituent subunits of the ubiquinol-cytochrome c reductase, which are imported by mitochondria, has allowed study of selected steps in the addressing of proteins to mitochondria and their intercompartmental sorting within the organelle. Recent developments are discussed.

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