Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology.

Kirk BW; Kuchta RD

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Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology.

机译：人DNA primase的Arg304是催化和NTP结合的关键因素：primase和X族聚合酶具有显着的序列同源性。

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Comparison of the amino acid sequences of eucaryotic DNA primase and the family X polymerases indicates that primase shares significant sequence homology with this family. With the use of DNA polymerase beta (pol beta) as a paradigm for family X polymerases, these homologies include both the catalytic core domain/subunit of each enzyme (31 kDa domain of pol beta and p49 subunit of primase) as well as the accessory domain/subunit (8 kDa domain of pol beta and p58 subunit of primase). To further explore these homologies as well as provide insights into the mechanism of primase, we generated three mutants (R304K, R304Q, and R304A) of the p49 subunit at an arginine that is highly conserved between primase and the eukaryotic family X polymerases. These mutations significantly decreased the rate of primer synthesis, due primarily to a decreased rate of initiation, and the extent of impairment correlated with the severity of the mutation (A > Q > K). R304 also contributes to efficient utilization of the NTP that will become the 5'-terminus of the new primer, and these effects are at least partially mediated through interactions with the phosphates of this NTP. The implications of these results with respect to the structure and biological role of primase, as well as its relationship to the family X polymerases, are discussed.

机译：真核DNA primase和X族聚合酶的氨基酸序列比较表明，primase与该家族有重要的序列同源性。通过使用DNA聚合酶beta（pol beta）作为X族聚合酶的范例，这些同源性既包括每种酶的催化核心结构域/亚基（pol beta的31 kDa结构域和primase的p49亚基），也包括附件结构域/亚基（pol beta的8 kDa结构域和primase的p58亚基）。为了进一步探索这些同源性并提供有关引发酶机理的见解，我们在精氨酸中产生了p49亚基的三个突变体（R304K，R304Q和R304A），该突变在引发酶和真核X族聚合酶之间高度保守。这些突变显着降低了引物合成的速率，这主要是由于起始速率降低，并且损伤程度与突变的严重程度相关（A> Q> K）。 R304还有助于有效利用NTP，该NTP将成为新引物的5'-末端，这些作用至少部分是通过与该NTP磷酸酯的相互作用介导的。讨论了这些结果对引发酶的结构和生物学作用及其与X族聚合酶的关系的影响。

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《Biochemistry》 |1999年第24期|共10页
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Kirk BW; Kuchta RD;
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正文语种 eng
中图分类生物化学;
关键词
Arginine; DNA Primase; Nucleotides; Sequence Homology; Amino Acid; DNA Polymerase beta; 精氨酸; DNA引发酶; 核苷酸类; 序列同源性; 氨基酸;

机译：Arginine;DNA Primase;Nucleotides;Sequence Homology;Amino Acid;DNA Polymerase beta;精氨酸;DNA引发酶;核苷酸类;序列同源性;氨基酸;

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1. Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology. [J] . Kirk BW, Kuchta RD Biochemistry . 1999,第24期

机译：人DNA primase的Arg304是催化和NTP结合的关键因素：primase和X族聚合酶具有显着的序列同源性。
2. The C-terminal Domain of the DNA Polymerase Catalytic Subunit Regulates the Primase and Polymerase Activities of the Human DNA Polymerase α-Primase Complex [J] . Yinbo Zhang, Andrey Baranovskiy, Tahir Tahirov, The Journal of biological chemistry . 2014,第32期

机译：DNA聚合酶催化亚单位的C末端结构域调节人DNA聚合酶α-丙酶复合物的基序和聚合酶活性
3. Polymerization of 2'-fluoro- and 2'-O-methyl-dNTPs by human DNA polymerase alpha, polymerase gamma, and primase. [J] . Richardson FC, Kuchta RD, Mazurkiewicz A, Biochemical Pharmacology . 2000,第9期

机译：人DNA聚合酶α，聚合酶γ和primase聚合2'-氟-和2'-O-甲基-dNTPs。
4. Towards an understanding of protein-protein interaction network hierarchies. Analysis of DnaN (β)-binding peptide motifs in members of protein families interacting with the eubacterial processivity clamp, the β subunit of DNA Polymerase III [C] . Brian P. Dalrymple, Gene Wijffels, Kritaya Kongsuwan, Asia-Pacific Bioinformatics Conference(APBC 2003); 200302; Adelaide(AU) . 2003

机译：对蛋白质-蛋白质相互作用网络层次结构的理解。蛋白质家族成员与DNA聚合酶III的优生过程性钳位相互作用的DnaN（β）结合肽基序分析
5. Immunoaffinity purification of the 180-kDa and 86-kDa subunits and in vitro reconstitution of the Saccharomyces cerevisiae DNA primase-DNA polymerase protein complex. [D] . Brooke, Richard Glenn. 1990

机译：180 kDa和86 kDa亚基的免疫亲和纯化和酿酒酵母DNA primase-DNA聚合酶蛋白复合物的体外重组。
6. The C-terminal Domain of the DNA Polymerase Catalytic Subunit Regulates the Primase and Polymerase Activities of the Human DNA Polymerase α-Primase Complex [O] . Yinbo Zhang, Andrey G. Baranovskiy, Tahir H. Tahirov, 2014

机译：DNA聚合酶催化亚基的C末端结构域调节人DNA聚合酶α-Primase复合物的启动酶和聚合酶活性。
7. Crystal structure of the C-terminal domain of human DNA primase large subunit: Implications for the mechanism of the primase—polymerase α switch [O] . Agarkar, Vinod B, Babayeva, Nigar D, Pavlov, Youri I, 2011

机译：人类DNA primase大亚基C末端结构域的晶体结构：对primase-polymeraseα开关机制的影响

Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology.

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