A novel fold in the TraI relaxase-helicase c-terminal domain is essential for conjugative DNA transfer.

Journal of Molecular Biology
Laura M GuogasMatthew R Redinbo

Abstract

TraI relaxase-helicase is the central catalytic component of the multiprotein relaxosome complex responsible for conjugative DNA transfer (CDT) between bacterial cells. CDT is a primary mechanism for the lateral propagation of microbial genetic material, including the spread of antibiotic resistance genes. The 2.4-A resolution crystal structure of the C-terminal domain of the multifunctional Escherichia coli F (fertility) plasmid TraI protein is presented, and specific structural regions essential for CDT are identified. The crystal structure reveals a novel fold composed of a 28-residue N-terminal alpha-domain connected by a proline-rich loop to a compact alpha/beta-domain. Both the globular nature of the alpha/beta-domain and the presence as well as rigidity of the proline-rich loop are required for DNA transfer and single-stranded DNA binding. Taken together, these data establish the specific structural features of this noncatalytic domain that are essential to DNA conjugation.

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Citations

Oct 12, 2010·Biomolecular NMR Assignments·Nathan T WrightJoel F Schildbach
Jun 6, 2014·Journal of Molecular Modeling·Nicholas J ClarkJoseph E Curtis
Oct 7, 2014·Journal of Molecular Biology·Yun PengJ N Mark Glover
May 23, 2012·Proteins·Nathan T WrightJoel F Schildbach
Jul 14, 2012·Molecular Microbiology·Joyce J W WongJ N Mark Glover
Aug 27, 2014·FEMS Microbiology Reviews·Elena CabezónIgnacio Arechaga
Nov 19, 2009·FEMS Microbiology Reviews·Fernando de la CruzEllen L Zechner
Jan 9, 2019·Biomolecular NMR Assignments·Bhattiprolu KrishnaKlaus Zangger
Jul 6, 2019·Nucleic Acids Research·Jan-Hendrik HeilersChris van der Does
Sep 24, 2020·Biomedicines·Nicholas BragagnoloGerald F Audette

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