دورية أكاديمية

Inorganic sulfur fixation via a new homocysteine synthase allows yeast cells to cooperatively compensate for methionine auxotrophy.

التفاصيل البيبلوغرافية
العنوان: Inorganic sulfur fixation via a new homocysteine synthase allows yeast cells to cooperatively compensate for methionine auxotrophy.
المؤلفون: Jason S L Yu, Benjamin M Heineike, Johannes Hartl, Simran K Aulakh, Clara Correia-Melo, Andrea Lehmann, Oliver Lemke, Federica Agostini, Cory T Lee, Vadim Demichev, Christoph B Messner, Michael Mülleder, Markus Ralser
المصدر: PLoS Biology, Vol 20, Iss 12, p e3001912 (2022)
بيانات النشر: Public Library of Science (PLoS), 2022.
سنة النشر: 2022
المجموعة: LCC:Biology (General)
مصطلحات موضوعية: Biology (General), QH301-705.5
الوصف: The assimilation, incorporation, and metabolism of sulfur is a fundamental process across all domains of life, yet how cells deal with varying sulfur availability is not well understood. We studied an unresolved conundrum of sulfur fixation in yeast, in which organosulfur auxotrophy caused by deletion of the homocysteine synthase Met17p is overcome when cells are inoculated at high cell density. In combining the use of self-establishing metabolically cooperating (SeMeCo) communities with proteomic, genetic, and biochemical approaches, we discovered an uncharacterized gene product YLL058Wp, herein named Hydrogen Sulfide Utilizing-1 (HSU1). Hsu1p acts as a homocysteine synthase and allows the cells to substitute for Met17p by reassimilating hydrosulfide ions leaked from met17Δ cells into O-acetyl-homoserine and forming homocysteine. Our results show that cells can cooperate to achieve sulfur fixation, indicating that the collective properties of microbial communities facilitate their basic metabolic capacity to overcome sulfur limitation.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1544-9173
1545-7885
Relation: https://doaj.org/toc/1544-9173; https://doaj.org/toc/1545-7885
DOI: 10.1371/journal.pbio.3001912
URL الوصول: https://doaj.org/article/4bafcd4cc0e6402c9e4cfcf9d4e05d8c
رقم الأكسشن: edsdoj.4bafcd4cc0e6402c9e4cfcf9d4e05d8c
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:15449173
15457885
DOI:10.1371/journal.pbio.3001912