Document Detail


Restriction endonucleases: natural and directed evolution.
MedLine Citation:
PMID:  22398859     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Type II restriction endonucleases (REs) are highly sequence-specific compared with other classes of nucleases. PD-(D/E)XK nucleases, initially represented by only type II REs, now comprise a large and extremely diverse superfamily of proteins and, although sharing a structurally conserved core, typically display little or no detectable sequence similarity except for the active site motifs. Sequence similarity can only be observed in methylases and few isoschizomers. As a consequence, REs are classified according to combinations of functional properties rather than on the basis of genetic relatedness. New alignment matrices and classification systems based on structural core connectivity and cleavage mechanisms have been developed to characterize new REs and related proteins. REs recognizing more than 300 distinct specificities have been identified in RE database (REBASE: http://rebase.neb.com/cgi-bin/statlist ) but still the need for newer specificities is increasing due to the advancement in molecular biology and applications. The enzymes have undergone constant evolution through structural changes in protein scaffolds which include random mutations, homologous recombinations, insertions, and deletions of coding DNA sequences but rational mutagenesis or directed evolution delivers protein variants with new functions in accordance with defined biochemical or environmental pressures. Redesigning through random mutation, addition or deletion of amino acids, methylation-based selection, synthetic molecules, combining recognition and cleavage domains from different enzymes, or combination with domains of additional functions change the cleavage specificity or substrate preference and stability. There is a growing number of patents awarded for the creation of engineered REs with new and enhanced properties.
Authors:
Richa Gupta; Neena Capalash; Prince Sharma
Related Documents :
18676669 - Isorenieratene biosynthesis in green sulfur bacteria requires the cooperative actions o...
8990219 - Cation-exchange hplc evaluated for presumptive identification of hemoglobin variants.
3098319 - Cloning and characterization of platelet factor 4 cdna derived from a human erythroleuk...
8161819 - Positive and negative regulatory elements of the rabbit embryonic epsilon-globin gene r...
9853679 - The cdna-derived amino acid sequence of indoleamine dioxygenase like-myoglobin from the...
14658229 - Genomic structure and characterisation of the promoter region of the human il-18 gene.
20093289 - The swedish new variant of chlamydia trachomatis: genome sequence, morphology, cell tro...
8621079 - Nucleotide sequence of the rhodobacter capsulatus hemh gene.
8809019 - A group i plant intron accumulates as circular rna forms with extensive 5' deletions in...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-3-8
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  -     ISSN:  1432-0614     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Department of Biotechnology, Panjab University, Chandigarh, India, 160014.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  A combined pharmacometric analysis of dabigatran etexilate in healthy volunteers and patients with a...
Next Document:  L: -Pantoyl lactone dehydrogenase from Rhodococcus erythropolis: genetic analyses and application to...