Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-beta-lactamases: a molecular and evolutionary study SCIE SCOPUS

Cited 15 time in WEB OF SCIENCE Cited 17 time in Scopus
Title
Dual activity of PNGM-1 pinpoints the evolutionary origin of subclass B3 metallo-beta-lactamases: a molecular and evolutionary study
Author(s)
Lee, Jung Hun; Takahashi, Masayuki; Jeon, Jeong Ho; Kang, Lin-Woo; Seki, Mineaki; Park, Kwang Seung; Hong, Myoung-Ki; Park, Yoon Sik; Kim, Tae Yeong; Karim, Asad Mustafa; Lee, Jung-Hyun; Nashimoto, Masayuki; Lee, Sang Hee
KIOST Author(s)
Lee, Jung Hyun(이정현)
Alternative Author(s)
이정현
Publication Year
2019-01
Abstract
Resistance to beta-lactams is one of the most serious problems associated with Gram-negative infections. beta-Lactamases are able to hydrolyze beta-lactams such as cephalosporins and/or carbapenems. Evolutionary origin of metallo-beta-lactamases (MBLs), conferring critical antibiotic resistance threats, remains unknown. We discovered PNGM-1, the novel subclass B3 MBL, in deep-sea sediments that predate the antibiotic era. Here, our phylogenetic analysis suggests that PNGM-1 yields insights into the evolutionary origin of subclass B3 MBLs. We reveal the structural similarities between tRNase Zs and PNGM-1, and demonstrate that PNGM-1 has both MBL and tRNase Z activities, suggesting that PNGM-1 is thought to have evolved from a tRNase Z. We also show kinetic and structural comparisons between PNGM-1 and other proteins including subclass B3 MBLs and tRNase Zs. These comparisons revealed that the B3 MBL activity of PNGM-1 is a promiscuous activity and subclass B3 MBLs are thought to have evolved through PNGM-1 activity.
ISSN
2222-1751
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/38875
DOI
10.1080/22221751.2019.1692638
Bibliographic Citation
Emerging Microbes and Infections, v.8, no.1, pp.1688 - 1700, 2019
Publisher
Nature Publishing Group
Keywords
Antimicrobial resistance; subclass B3 metallo-beta-lactamase; tRNase Z; dual activity; structure and evolutionary origin
Type
Article
Language
English
Document Type
Article
Publisher
Nature Publishing Group
Files in This Item:
There are no files associated with this item.

qrcode

Items in ScienceWatch@KIOST are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse