Structural features of a minimal intact methyltransferase of a type I restriction-modification system.

Autor: Seo PW; Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea., Hofmann A; Department of Veterinary Biosciences, Melbourne Veterinary School, The University of Melbourne, Parkville, Victoria 3010, Australia; Max Rubner-Institut, Federal Research Institute of Nutrition and Food, 95326 Kulmbach, Germany., Kim JH; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea; Department of Chemical Engineering, Kumoh National Institute of Technology, 61, Daehak-ro, Gumi, Gyeongbuk 39177, Republic of Korea., Hwangbo SA; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea; Department of Life Sciences and Institute of Membrane Proteins, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea., Kim JH; Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea., Kim JW; Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea., Huynh TYL; Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea., Choy HE; Department of Microbiology, Basic Medical Research Building, Chonnam National University Medical College, Hwasun, Jeonnam 58128, Republic of Korea., Kim SJ; Department of Integrative Food, Bioscience and Biotechnology, Chonnam National University, Gwangju 61186, Republic of Korea., Lee J; Department of Life Sciences and Institute of Membrane Proteins, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea., Lee JO; Department of Life Sciences and Institute of Membrane Proteins, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea., Jin KS; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea. Electronic address: jinks@postech.ac.kr., Park SY; Pohang Accelerator Laboratory, Pohang University of Science and Technology, Pohang, Gyeongbuk 37673, Republic of Korea. Electronic address: navypsy@postech.ac.kr., Kim JS; Department of Chemistry, Chonnam National University, Gwangju 61186, Republic of Korea. Electronic address: jsunkim@chonnam.ac.kr.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2022 May 31; Vol. 208, pp. 381-389. Date of Electronic Publication: 2022 Mar 23.
DOI: 10.1016/j.ijbiomac.2022.03.115
Abstrakt: Type I restriction-modification enzymes are oligomeric proteins composed of methylation (M), DNA sequence-recognition (S), and restriction (R) subunits. The different bipartite DNA sequences of 2-4 consecutive bases are recognized by two discerned target recognition domains (TRDs) located at the two-helix bundle of the two conserved regions (CRs). Two M-subunits and a single S-subunit form an oligomeric protein that functions as a methyltransferase (M 2 S 1 MTase). Here, we present the crystal structure of the intact MTase from Vibrio vulnificus YJ016 in complex with the DNA-mimicking Ocr protein and the S-adenosyl-L-homocysteine (SAH). This MTase includes the M-domain with a helix tail (M-tail helix) and the S 1/2 -domain of a TRD and a CR α-helix. The Ocr binds to the cleft of the TRD surface and SAH is located in the pocket within the M-domain. The solution- and negative-staining electron microscopy-based reconstructed (M 1 S 1/2 ) 2 structure reveals a symmetric (S 1/2 ) 2 assembly using two CR-helices and two M-tail helices as a pivot, which is plausible for recognizing two DNA regions of same sequence. The conformational flexibility of the minimal M 1 S 1/2 MTase dimer indicates a particular state resembling the structure of M 2 S 1 MTases.
(Copyright © 2022. Published by Elsevier B.V.)
Databáze: MEDLINE
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