cleavage site


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re·stric·tion site

a site in nucleic acid in which the bordering bases are of such a type as to leave them vulnerable to the cleaving action of an endonuclease.
Synonym(s): cleavage site

re·stric·tion site

(rĕ-strik'shŭn sīt)
A site in nucleic acid in which the bordering bases are of such a type as to leave them vulnerable to the cleaving action of an endonuclease.
Synonym(s): cleavage site.

cleavage site

The location on a polypeptide molecule where peptide bonds are broken down by hydrolysis.
See also: site

cleavage

1. division into distinct parts, e.g. the double helix.
2. the early successive splitting of a fertilized ovum into smaller cells (blastomeres) by mitosis. See also holoblastic, meroblastic.

cleavage site
the places on a strand of DNA where the restriction enzyme cleaves the DNA.
References in periodicals archive ?
The cleavage site motif 112-R-R-Q-K-R-F117 was present in AW-14 strain, which is typical of vNDV strain (Miller et al.
Finally, the third experiment applies the HyRPNI algorithm to the cleavage site prediction problem on polyproteins from genomes of Potyviridae family.
A red bar in the hemagglutinin gene of the HPAI virus indicates the insertion at the hemagglutinin cleavage site.
Moreover, just a two- nucleotide change at the F protein cleavage site is enough to change the virus from a low virulent to a virulent strain (Gould et al.
Glycosylation residues in the region of the proBNP molecule close to the cleavage site inhibit the processing of proBNP.
Despite multiple computational tools for predicting a signal peptide and assessment of its cleavage site by signal peptidase, SignalP is one of the best and most reliable tools in this regard with 85% accuracy in prediction of a potential signal peptide.
The insert was flanked by the natural P1/HC-Pro cleavage site and an introduced 7 amino acids which are recognized by the PRSV NIa proteinase (Yeh et al.
1, steps vii and viii) to yield HA1 (327 amino acids) and HA2 (222 amino acids), which are still linked by a disulphide bond; most influenza viruses contain a single basic amino acid residue (arginine, rarely lysine) at the cleavage site.
Protein binding was noted in the extreme boundaries of this region, but not in an internal region previously described as both a topo II cleavage site and a DNase I hypersensitive site.
Genes of interest are cloned into the multiple cloning site of the Vector System just downstream of the p26 or alpha crystallin type protein and a thrombin cleavage site.
The isolated virus was identified as a highly pathogenic H5N1, with a hemagglutinin proteolytic cleavage site deduced amino acid sequence of QREKRKKR/ GLFGAIAG.