Spectroscopic Signature of the Steric Strains in an Escherichia coli RNase HI Cavity-Filling Destabilized Mutant Protein

2019 ◽  
Vol 124 (1) ◽  
pp. 91-100 ◽  
Author(s):  
Chikashi Ota ◽  
Hikari Suzuki ◽  
Shun-ichi Tanaka ◽  
Kazufumi Takano
Keyword(s):  
Escherichia Coli ◽  
Mutant Protein ◽  
Rnase Hi ◽  
Cavity Filling

Protein Core Adaptability: Crystal Structures of the Cavity-Filling Variants of Escherichia coli RNase HI

2010 ◽  
Vol 17 (9) ◽  
pp. 1163-1169 ◽  
Author(s):  
Masaki Tanaka ◽  
Hyongi Chon ◽  
Clement Angkawidjaja ◽  
Yuichi Koga ◽  
Kazufumi Takano ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Crystal Structures ◽  
Protein Core ◽  
Rnase Hi ◽  
Cavity Filling

scholarly journals Competitive binding of MatP and topoisomerase IV to the MukB dimerization hinge

2021 ◽  
Author(s):  
Gemma L. M. Fisher ◽  
Jani R. Bolla ◽  
Karthik V. Rajasekar ◽  
Jarno Mäkelä ◽  
Rachel Baker ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Competitive Binding ◽  
Mutant Protein ◽  
Chromosomal Distribution ◽  
Topoisomerase Iv ◽  
Binding Interface ◽  
Cellular Localisation ◽  
Chromosome Organisation

ABSTRACTSMC complexes have ubiquitous roles in chromosome organisation. In Escherichia coli, the interplay between the SMC complex, MukBEF, and matS-bound MatP in the replication termination region, ter, results in depletion of MukBEF from ter, thus promoting chromosome individualisation by directing replichores to separate cell halves. MukBEF also interacts with topoisomerase IV ParC2E2 heterotetramers, to direct its chromosomal distribution to mirror that of MukBEF, thereby facilitating coordination between chromosome organisation and decatenation by topoisomerase IV. Here we demonstrate that the MukB dimerization hinge binds ParC and MatP with the same dimer to dimer stoichiometry. MatP and ParC have an overlapping binding interface on the MukB hinge, leading to their mutually exclusive binding. Furthermore, the MukB hinge fails to stably associate with matS-bound MatP, while MatP mutants deficient in matS binding are impaired in MukB hinge binding, demonstrating that mats competes with the hinge for MatP binding. Cells expressing MukBEF complexes containing a mutation in the MukB hinge interface for ParC/MatP binding are deficient in ParC binding in vivo, despite having a Muk+ topoisomerase IV+ phenotype. This mutant protein is also impaired in MatP binding in vitro, and cells expressing this variant exhibit a MukBEF cellular localisation consistent with impaired MatP binding.

scholarly journals RNase HI overproduction is required for efficient full-length RNA synthesis in the absence of topoisomerase I in Escherichia coli

2004 ◽  
Vol 54 (1) ◽  
pp. 198-211 ◽  
Author(s):  
Imad Baaklini ◽  
Chadi Hraiky ◽  
Fabien Rallu ◽  
Yuk-Ching Tse-Dinh ◽  
Marc Drolet
Keyword(s):  
Escherichia Coli ◽  
Topoisomerase I ◽  
Rna Synthesis ◽  
Full Length ◽  
Rnase Hi

scholarly journals RnlB Antitoxin of the Escherichia coli RnlA-RnlB Toxin–Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity

Toxins ◽  
2017 ◽  
Vol 9 (1) ◽  
pp. 29 ◽  
Author(s):  
Kenta Naka ◽  
Dan Qi ◽  
Tetsuro Yonesaki ◽  
Yuichi Otsuka
Keyword(s):  
Escherichia Coli ◽  
Rnase Hi

How RNase HI (Escherichia coli) promoted site-selective hydrolysis works on RNA in duplex with carba-LNA and LNA substituted antisense strands in an antisense strategy context?

2017 ◽  
Vol 13 (5) ◽  
pp. 921-938
Author(s):  
Oleksandr Plashkevych ◽  
Qing Li ◽  
Jyoti Chattopadhyaya
Keyword(s):  
Escherichia Coli ◽  
Nucleic Acid ◽  
Kinetic Study ◽  
Rnase H ◽  
Locked Nucleic Acid ◽  
Cleavage Sites ◽  
Selective Hydrolysis ◽  
Rnase Hi ◽  
Site Selective

Kinetic study of 36 AON–RNA heteroduplexes single modified by locked nucleic acid (LNA) or by carba-LNA show site-dependent modulation of RNase H promoted cleavage of RNA strand by 2 to 5 fold with preferential 5′-GpN-3′ cleavage sites, giving up to 70% of the products.

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