Abstract: The disclosure provides a high-fidelity polymerase with preference for gapped DNA and use thereof. The Klenow fragment (KlenDr) derived from Deinococcus radiodurans DNA polymerase I, which has the high-fidelity polymerization characteristics, is independent of 3?-5? proofreading exonuclease activity, has the preference for binding gapped DNA, and is different from the existing commercial high-fidelity polymerase. Due to the specific affinity of KlenDr to gapped DNA substrate, the 3? end of the forward primer will not be cut off, and the downstream nucleotide chain is rarely replaced.

Abstract: A DNA methyltransferase is derived from Deinococcus radiodurans and has a typical conservative structural domain of DNA methyltransferase. The DNA methyltransferase includes: an AdoMet binding region containing a “FxGxG” conservative sequence, a target sequence recognition region and a catalytic region containing a “TSPPY” conservative sequence sequentially from N-terminal to C-terminal; and belongs to ?-type DNA methyltransferase category. The recognized substrate DNA conservative sequence is 5?-CCGCGG-3?, a methylation modified position is N4 site of second cytosine to generate a 4mC type modified base, and an optimum temperature for methylated reaction is in a range of 25-37° C. The DNA methyltransferase can specific-recognize the conservative motif of “CCGCGG” and methylate the N4 site of the second cytosine to produce the 4mC modified base, which is a N4-Cytosine DNA methyltransferase.

Abstract: The disclosure provides a high-fidelity polymerase with preference for gapped DNA and use thereof. The Klenow fragment (KlenDr) derived from Deinococcus radiodurans DNA polymerase I, which has the high-fidelity polymerization characteristics, is independent of 3?-5? proofreading exonuclease activity, has the preference for binding gapped DNA, and is different from the existing commercial high-fidelity polymerase. Due to the specific affinity of KlenDr to gapped DNA substrate, the 3? end of the forward primer will not be cut off, and the downstream nucleotide chain is rarely replaced.

Abstract: The present invention relates to a polypeptide having protease activity comprising a zinc finger protease domain, a helix-turn-helix domain and a GAF domain. The core protein sequence of the protease is shown as SEQ ID NO: 1. The invention also relates to optimized reaction conditions for the protease and methods of increasing the protease activity.

Abstract: The present invention relates to a polypeptide having protease activity comprising a zinc finger protease domain, a helix-turn-helix domain and a GAF domain. The core protein sequence of the protease is shown as SEQ ID NO: 1. The invention also relates to optimized reaction conditions for the protease and methods of increasing the protease activity.