The N-Terminal Domain of the Escherichia coli PriA Helicase Contains Both the DNA- and Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors

Szymanski MR; Bujalowski PJ; Jezewska MJ; Gmyrek AM; Bujalowski W

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The N-Terminal Domain of the Escherichia coli PriA Helicase Contains Both the DNA- and Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors

机译：大肠杆菌的N-末端结构域含有DNA和核苷酸结合位点。核苷酸辅因子的域-DNA相互作用的能量学和骨质蛋白

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Functional interactions of the Escherichia coli PriA helicase 181N-terminal domain with the DNA and nucleotide cofactors have been quantitatively examined. The isolated 181N-terminal domain forms a stable dimer in solution, most probably reflecting the involvement of the domain in specific cooperative interactions of the intact PriA protein-double-stranded DNA (dsDNA) complex. Only one monomer of the domain dimer binds the DNA; i.e., the dimer has one effective DNA-binding site. Although the total site size of the dimer-single-stranded DNA (ssDNA) complex is similar to 13 nucleotides, the DNA-binding subsite engages in direct interactions with approximately five nucleotides. A small number of interacting nucleotides indicates that the DNA-binding subsites of the PriA helicase, i.e., the strong subsite on the helicase domain and the weak subsite on the N-terminal domain, are spatially separated in the intact enzyme. Contrary to current views, the subsite has an only slight preference for the 3'-end OH group of the ssDNA and lacks any significant base specificity, although it has a significant dsDNA affinity. Unlike the intact helicase, the DNA-binding subsite of the isolated domain is in an open conformation, indicating the presence of the direct helicase domain-N-terminal domain interactions. The discovery that the 181N-terminal domain possesses a nucleotide-binding site places the allosteric, weak nucleotide-binding site of the intact PriA on the N-terminal domain. The specific effect of ADP on the domain DNA-binding subsite indicates that in the intact helicase, the bound ADP not only opens the DNA-binding subsite but also increases its intrinsic DNA affinity.

机译：已经定量地检查了与DNA和核苷酸辅因子的大肠杆菌类大肠杆菌PRIA Helicate 181n-末端结构域的功能相互作用。孤立的181n-末端结构域在溶液中形成稳定的二聚体，最可能反映结构域在完整的PRIA蛋白 - 双链DNA（DSDNA）复合物的特定合作相互作用中。只有一个畴二聚体的单体结合DNA;即，二聚体具有一个有效的DNA结合位点。尽管二聚体 - 单链DNA（SSDNA）复合物的总位点尺寸类似于13个核苷酸，但DNA结合子部分与大约五个核苷酸的直接相互作用。少量的相互作用核苷酸表明，PRIA螺旋酶的DNA结合底座，即螺旋酶结构域上的强子岩和N-末端结构域的弱子部分，在完整的酶中分离。与目前的视图相反，底座对SSDNA的3'-End OH组仅略微偏好，并且缺乏任何显着的基本特异性，尽管它具有重要的DSDNA亲和力。与完整的旋光酶不同，分离结构域的DNA结合子部分是开放的构象，表明存在直接螺旋酶结构域-N-末端结构域相互作用。发现181n-末端结构域具有核苷酸结合位点的末端结合位点，将完整的PRIA的变形弱核苷酸结合位点放在N-末端结构域上。 ADP对域DNA结合底座的特异性效果表明，在完整的旋光酶中，结合的ADP不仅打开了DNA结合底座，而且增加了其内在的DNA亲和力。

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《Biochemistry》 |2011年第43期|共17页
作者
Szymanski MR; Bujalowski PJ; Jezewska MJ; Gmyrek AM; Bujalowski W;
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作者单位

Department of Biochemistry and Molecular Biology Department of Obstetrics and Gynecology The Sealy Center for Structural Biology and The Sealy Center for Cancer Cell Biology The University of Texas Medical Branch at Galveston 301 University Boulevard;

Department of Biochemistry and Molecular Biology Department of Obstetrics and Gynecology The Sealy Center for Structural Biology and The Sealy Center for Cancer Cell Biology The University of Texas Medical Branch at Galveston 301 University Boulevard;

Department of Biochemistry and Molecular Biology Department of Obstetrics and Gynecology The Sealy Center for Structural Biology and The Sealy Center for Cancer Cell Biology The University of Texas Medical Branch at Galveston 301 University Boulevard;

Department of Biochemistry and Molecular Biology Department of Obstetrics and Gynecology The Sealy Center for Structural Biology and The Sealy Center for Cancer Cell Biology The University of Texas Medical Branch at Galveston 301 University Boulevard;

Department of Biochemistry and Molecular Biology Department of Obstetrics and Gynecology The Sealy Center for Structural Biology and The Sealy Center for Cancer Cell Biology The University of Texas Medical Branch at Galveston 301 University Boulevard;

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正文语种 eng
中图分类生物化学;
关键词
N-Terminal; Escherichia; Interactions;

机译：N-终端;大肠杆菌;互动;

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专利

1. The N-Terminal Domain of the Escherichia coli PriA Helicase Contains Both the DNA- and Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors [J] . Szymanski MR, Bujalowski PJ, Jezewska MJ, Biochemistry . 2011,第43期

机译：大肠杆菌的N-末端结构域含有DNA和核苷酸结合位点。核苷酸辅因子的域-DNA相互作用的能量学和骨质蛋白
2. Kinetic mechanisms of the nucleotide cofactor binding to the strong and weak nucleotide-binding site of the Escherichia coli PriA helicase. 2 [J] . Lucius AL, Jezewska MJ, Roychowdhury A, Biochemistry . 2006,第23期

机译：核苷酸辅因子与大肠杆菌PriA解旋酶强和弱核苷酸结合位点结合的动力学机制。 2
3. The Escherichia coli PriA helicase-double-stranded DNA complex: location of the strong DNA-binding subsite on the helicase domain of the protein and the affinity control by the two nucleotide-binding sites of the enzyme. [J] . Szymanski MR, Jezewska MJ, Bujalowski W Journal of Molecular Biology . 2010,第2期

机译：大肠杆菌PriA解旋酶双链DNA复合物：蛋白质的解旋酶结构域上强DNA结合亚位点的位置，并通过酶的两个核苷酸结合位点控制亲和力。
4. Regulation of chromosomal DNA replication in Escherichia coli: I. Function of an N-terminal domain in DnaA oligomer formation. II. Biochemical and genetic studies of hyperactive dnaA alleles [D] . Simmons, Lyle Adair 2003

机译：大肠杆菌中染色体DNA复制的调节：I. DnaA寡聚物形成中的N末端结构域的功能。二。过度活跃的dnaA等位基因的生化和遗传研究
5. The N-Terminal Domain of the E. coli PriA Helicase Contains Both the DNA- and the Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors [O] . Michal R. Szymanski, Paul J. Bujalowski, Maria J. Jezewska, -1

机译：大肠杆菌Pria Helicase的N-末端结构域含有DNA和核苷酸结合位点。核苷酸辅因子的区域-DNA相互作用的能量学和骨核苷酸的变构效果
6. The Escherichia coli PriA Helicase–Double-Stranded DNA Complex: Location of the Strong DNA-Binding Subsite on the Helicase Domain of the Protein and the Affinity Control by the Two Nucleotide-Binding Sites of the Enzyme [O] . Michal R. Szymanski, Maria J. Jezewska, Wlodzimierz Bujalowski 2010

机译：大肠杆菌癌直升机 - 双链DNA复合物：蛋白质的螺旋酶结构域上的强DNA结合子部分的位置和酶的两个核苷酸结合位点的亲和控制

The N-Terminal Domain of the Escherichia coli PriA Helicase Contains Both the DNA- and Nucleotide-Binding Sites. Energetics of Domain-DNA Interactions and Allosteric Effect of the Nucleotide Cofactors

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