期刊
SCIENCE
卷 371, 期 6533, 页码 1010-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aay2784
关键词
-
资金
- National Science Foundation (NSF) [MCB-1714723]
- National Institutes of Health (NIH) [R01 GM60595]
- National Energy Research Scientific Computing Center (NERSC), a U.S. Department of Energy (DOE) Office of Science User Facility [DE-AC02-05CH11231]
- FICUS program [503369]
- U.S. DOE, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- DOE Office of Biological and Environmental Research
- NIH, National Institute of General Medical Sciences (NIGMS) [P41GM103393]
- NSF
- Stanford Medical Scientist Training Program
- Stanford Interdisciplinary Graduate Fellowship
- NSF Graduate Research Fellowship
- Human Frontiers Postdoctoral Fellowship
This study reveals the molecular and evolutionary mechanisms of enzyme temperature adaptation, identifying that temperature adaptation in KSI primarily comes from a single residue change with limited, local epistasis. Residues associated with organismal growth temperature are also found across diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. The study assesses residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.
The mechanisms that underly the adaptation of enzyme activities and stabilities to temperature are fundamental to our understanding of molecular evolution and how enzymes work. Here, we investigate the molecular and evolutionary mechanisms of enzyme temperature adaption, combining deep mechanistic studies with comprehensive sequence analyses of thousands of enzymes. We show that temperature adaptation in ketosteroid isomerase (KSI) arises primarily from one residue change with limited, local epistasis, and we establish the underlying physical mechanisms. This residue change occurs in diverse KSI backgrounds, suggesting parallel adaptation to temperature. We identify residues associated with organismal growth temperature across 1005 diverse bacterial enzyme families, suggesting widespread parallel adaptation to temperature. We assess the residue properties, molecular interactions, and interaction networks that appear to underly temperature adaptation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据