Restriction endonuclease, type I, HsdR
InterPro Protein Domain record
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description
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<p>There are four classes of restriction endonucleases: types I, II,III and IV. All types of enzymes recognise specific short DNA sequences and carry out the endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates. They differ in their recognition sequence, subunit composition, cleavage position, and cofactor requirements [<cite idref="PUB00035705"/>, <cite idref="PUB00035707"/>], as summarised below:</p><p> <ul><li>Type I enzymes (<db_xref db="EC" dbkey="3.1.21.3"/>) cleave at sites remote from recognition site; require both ATP and S-adenosyl-L-methionine to function; multifunctional protein with both restriction and methylase (<db_xref db="EC" dbkey="2.1.1.72"/>) activities.</li><li>Type II enzymes (<db_xref db="EC" dbkey="3.1.21.4"/>) cleave within or at short specific distances from recognition site; most require magnesium; single function (restriction) enzymes independent of methylase.</li><li>Type III enzymes (<db_xref db="EC" dbkey="3.1.21.5"/>) cleave at sites a short distance from recognition site; require ATP (but doesn't hydrolyse it); S-adenosyl-L-methionine stimulates reaction but is not required; exists as part of a complex with a modification methylase methylase (<db_xref db="EC" dbkey="2.1.1.72"/>).</li><li>Type IV enzymes target methylated DNA.</li></ul> </p><p>Type I restriction endonucleases are components of prokaryotic DNA restriction-modification mechanisms that protects the organism against invading foreign DNA. Type I enzymes have three different subunits subunits - M (modification), S (specificity) and R (restriction) - that form multifunctional enzymes with restriction (<db_xref db="EC" dbkey="3.1.21.3"/>), methylase (<db_xref db="EC" dbkey="2.1.1.72"/>) and ATPase activities [<cite idref="PUB00035705"/>, <cite idref="PUB00035706"/>]. The S subunit is required for both restriction and modification and is responsible for recognition of the DNA sequence specific for the system. The M subunit is necessary for modification, and the R subunit is required for restriction. These enzymes use S-Adenosyl-L-methionine (AdoMet) as the methyl group donor in the methylation reaction, and have a requirement for ATP. They recognise asymmetric DNA sequences split into two domains of specific sequence, one 3-4 bp long and another 4-5 bp long, separated by a nonspecific spacer 6-8 bp in length. Cleavage occurs a considerable distance from the recognition sites, rarely less than 400 bp away and up to 7000 bp away. Adenosyl residues are methylated, one on each strand of the recognition sequence. These enzymes are widespread in eubacteria and archaea. In enteric bacteria they have been subdivide into four families: types IA, IB, IC and ID.</p><p>This entry represents the R subunit (HsdR) of type I restriction endonucleases. The R protein (HsdR) is required for both nuclease and ATPase activity [<cite idref="PUB00020851"/>, <cite idref="PUB00019722"/>, <cite idref="PUB00019721"/>]. Members of this family are assumed to differ from each other in DNA site specificity. </p>
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Restriction endonuclease, type I, HsdR
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