Origin of complexity in haemoglobin evolution

doi:10.1038/s41586-020-2292-y

GSTDTAP > 地球科学

DOI	10.1038/s41586-020-2292-y
	Origin of complexity in haemoglobin evolution
	Cheema, Suraj S.1; Kwon, Daewoong 2,12; Shanker, Nirmaan 1,2; dos Reis, Roberto 3; Hsu, Shang-Lin 3,7; Xiao, Jun 4; Zhang, Haigang 5; Wagner, Ryan 5; Datar, Adhiraj 1,2; McCarter, Margaret R.6; Serrao, Claudy R.2; Yadav, Ajay K.2; Karbasian, Golnaz 2; Hsu, Cheng-Hsiang 2; Tan, Ava J.2; Wang, Li-Chen 1; Thakare, Vishal 1; Zhang, Xiang 4; Mehta, Apurva 8; Karapetrova, Evguenia 9; Chopdekar, Rajesh, V 10; Shafer, Padraic 10; Arenholz, Elke 10,11; Hu, Chenming 2; Proksch, Roger 5; Ramesh, Ramamoorthy 1,6; Ciston, Jim 3; Salahuddin, Sayeef 2,7
	2020-04-01
发表期刊	NATURE
ISSN	0028-0836
EISSN	1476-4687
出版年	2020
文章类型	Article;Early Access
语种	英语
国家	USA; England; Germany
英文关键词	Most proteins associate into multimeric complexes with specific architectures(1,2), which often have functional properties such as cooperative ligand binding or allosteric regulation(3). No detailed knowledge is available about how any multimer and its functions arose during evolution. Here we use ancestral protein reconstruction and biophysical assays to elucidate the origins of vertebrate haemoglobin, a heterotetramer of paralogous alpha- and beta-subunits that mediates respiratory oxygen transport and exchange by cooperatively binding oxygen with moderate affinity. We show that modern haemoglobin evolved from an ancient monomer and characterize the historical ' missing link' through which the modern tetramer evolved-a noncooperative homodimer with high oxygen affinity that existed before the gene duplication that generated distinct alpha- and beta-subunits. Reintroducing just two post-duplication historical substitutions into the ancestral protein is sufficient to cause strong tetramerization by creating favourable contacts with more ancient residues on the opposing subunit. These surface substitutions markedly reduce oxygen affinity and even confer cooperativity, because an ancient linkage between the oxygen binding site and the multimerization interface was already an intrinsic feature of the protein' s structure. Our findings establish that evolution can produce new complex molecular structures and functions via simple genetic mechanisms that recruit existing biophysical features into higher-level architectures. Experimental analysis of reconstructed ancestral globins reveals that haemoglobin' s complex tetrameric structure and oxygen-binding functions evolved by simple genetic and biophysical mechanisms.
领域	地球科学 ; 气候变化 ; 资源环境
收录类别	SCI-E
WOS记录号	WOS:000534879300001
WOS关键词	3-DIMENSIONAL FOURIER SYNTHESIS ; LIGAND-BINDING ; GLOBIN GENE ; PROTEIN ; ALPHA ; DIVERSIFICATION ; RESOLUTION ; OXYGEN ; CYTOGLOBIN ; MYOGLOBIN
WOS类目	Multidisciplinary Sciences
WOS研究方向	Science & Technology - Other Topics
引用统计	被引频次：68[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://119.78.100.173/C666/handle/2XK7JSWQ/281291
专题	地球科学资源环境科学气候变化
作者单位	1.Univ Calif Berkeley, Dept Mat Sci & Engn, Berkeley, CA 94720 USA; 2.Univ Calif Berkeley, Dept Elect Engn & Comp Sci, Berkeley, CA 94720 USA; 3.Lawrence Berkeley Natl Lab, Mol Foundry, Natl Ctr Electron Microscopy, Berkeley, CA USA; 4.Univ Calif Berkeley, Nanoscale Sci & Engn Ctr, Berkeley, CA 94720 USA; 5.Oxford Instruments, Asylum Res, Santa Barbara, CA USA; 6.Univ Calif Berkeley, Dept Phys, Berkeley, CA 94720 USA; 7.Lawrence Berkeley Natl Lab, Mat Sci Div, Berkeley, CA 94720 USA; 8.SLAC Natl Accelerator Lab, Stanford Synchrotron Radiat Lightsource, Menlo Pk, CA USA; 9.Argonne Natl Lab, Adv Photon Source, Argonne, IL 60439 USA; 10.Lawrence Berkeley Natl Lab, Adv Light Source, Berkeley, CA USA; 11.Cornell Univ, Cornell High Energy Synchrotron Source, Ithaca, NY 14853 USA; 12.Inha Univ, Dept Elect Engn, Incheon, South Korea
推荐引用方式 GB/T 7714	Cheema, Suraj S.,Kwon, Daewoong,Shanker, Nirmaan,et al. Origin of complexity in haemoglobin evolution[J]. NATURE,2020.
APA	Cheema, Suraj S..,Kwon, Daewoong.,Shanker, Nirmaan.,dos Reis, Roberto.,Hsu, Shang-Lin.,...&Salahuddin, Sayeef.(2020).Origin of complexity in haemoglobin evolution.NATURE.
MLA	Cheema, Suraj S.,et al."Origin of complexity in haemoglobin evolution".NATURE (2020).