The regulation mechanism of the C-terminus of RecA proteins during DNA strand-exchange process

被引:3
|
作者
Fan, Hsiu-Fang [1 ,2 ,3 ]
Su, Shu [4 ,5 ]
机构
[1] Natl Sun Yat Sen Univ, Inst Med Sci & Technol, Kaohsiung, Taiwan
[2] Natl Sun Yat Sen Univ, Dept Chem, Kaohsiung, Taiwan
[3] Natl Sun Yat Sen Univ, Aerosol Sci Res Ctr, Kaohsiung, Taiwan
[4] Natl Yang Ming Univ, Dept Life Sci, Taipei, Taiwan
[5] Natl Yang Ming Univ, Inst Genome Sci, Taipei, Taiwan
关键词
TETHERED PARTICLE MOTION; DEINOCOCCUS-RADIODURANS; HOMOLOGOUS RECOMBINATION; FILAMENT DYNAMICS; BINDING; SITE; KINETICS; ABSENCE; DOMAIN; CRE;
D O I
10.1016/j.bpj.2021.06.004
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
The C-terminus of Escherichia coli RecA protein can affect the DNA binding affinity, interact with accessory proteins, and regulate the RecA activity. A substantial upward shift in the pH-reaction profile of RecA-mediated DNA strand-exchange reactions was observed for C-terminal-truncated E. coli Delta C17 RecA, Deinococcus radiodurans RecA, and Deinococcus ficus RecA. Here, the process of RecA-mediated strand exchange from the beginning to the end was investigated with florescence resonance energy transfer and tethered particle motion experiments to determine the detailed regulation mechanism. RecA proteins with a shorter C-terminus possess more stable nuclei, higher DNA binding affinities, and lower protonation requirements for the formation of nucleoprotein filaments. Moreover, more stable synaptic complexes in the homologous sequence searching process were also observed for RecA proteins with a shorter C-terminus. Our results suggest that the C-terminus of RecA proteins regulates not only the formation of RecA nucleoprotein filaments but also the entrance of secondary DNA into RecA nucleoprotein filaments.
引用
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页码:3166 / 3179
页数:14
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