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科学家利用岩石中微生物微量元素揭示地球生命起源 快报文章
地球科学快报,2022年第18期
作者:  刘文浩
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Biogeochemical  MTB  origin of life  
A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds 期刊论文
NATURE, 2020, 580 (7803) : 409-+
作者:  Al-Shayeb, Basem;  Sachdeva, Rohan;  Chen, Lin-Xing;  Ward, Fred;  Munk, Patrick;  Devoto, Audra;  Castelle, Cindy J.;  Olm, Matthew R.;  Bouma-Gregson, Keith;  Amano, Yuki;  He, Christine;  Meheust, Raphael;  Brooks, Brandon;  Thomas, Alex;  Levy, Adi;  Matheus-Carnevali, Paula;  Sun, Christine;  Goltsman, Daniela S. A.;  Borton, Mikayla A.;  Sharrar, Allison;  Jaffe, Alexander L.;  Nelson, Tara C.;  Kantor, Rose;  Keren, Ray;  Lane, Katherine R.;  Farag, Ibrahim F.;  Lei, Shufei;  Finstad, Kari;  Amundson, Ronald;  Anantharaman, Karthik;  Zhou, Jinglie;  Probst, Alexander J.;  Power, Mary E.;  Tringe, Susannah G.;  Li, Wen-Jun;  Wrighton, Kelly;  Harrison, Sue;  Morowitz, Michael;  Relman, David A.;  Doudna, Jennifer A.;  Lehours, Anne-Catherine;  Warren, Lesley;  Cate, Jamie H. D.;  Santini, Joanne M.;  Banfield, Jillian F.
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Mycobacterium tuberculosis (Mtb) is an obligate human pathogen and the causative agent of tuberculosis(1-3). Although Mtb can synthesize vitamin B-12 (cobalamin) de novo, uptake of cobalamin has been linked to pathogenesis of tuberculosis2. Mtb does not encode any characterized cobalamin transporter(4-6)  however, the gene rv1819c was found to be essential for uptake of cobalamin(1). This result is difficult to reconcile with the original annotation of Rv1819c as a protein implicated in the transport of antimicrobial peptides such as bleomycin(7). In addition, uptake of cobalamin seems inconsistent with the amino acid sequence, which suggests that Rv1819c has a bacterial ATP-binding cassette (ABC)-exporter fold1. Here, we present structures of Rv1819c, which reveal that the protein indeed contains the ABC-exporter fold, as well as a large water-filled cavity of about 7,700 angstrom(3), which enables the protein to transport the unrelated hydrophilic compounds bleomycin and cobalamin. On the basis of these structures, we propose that Rv1819c is a multi-solute transporter for hydrophilic molecules, analogous to the multidrug exporters of the ABC transporter family, which pump out structurally diverse hydrophobic compounds from cells(8-11).