IHB OpenIR  > 水生生物分子与细胞生物学研究中心  > 期刊论文
Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets
Kim, Youngchang1,2; Ye, Zi3; Joachimiak, Grazyna1,2; Videau, Patrick4; Young, Jasmine4; Hurd, Kathryn4; Callahan, Sean M.4; Gornicki, Piotr5; Zhao, Jindong3; Haselkorn, Robert5; Joachimiak, Andrzej1,2,6; Haselkorn, R (reprint author), Univ Chicago, Dept Mol Genet & Cell Biol, 920 E 58Th St, Chicago, IL 60637 USA.
2013-05-07
Source PublicationPROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
ISSN0027-8424
Volume110Issue:19Pages:E1716-E1723
AbstractHetR is an essential regulator of heterocyst development in cyanobacteria. Many mutations in HetR render Anabaena incapable of nitrogen fixation. The protein binds to a DNA palindrome upstream of hetP and other genes. We have determined the crystal structures of HetR complexed with palindromic DNA targets, 21, 23, and 29 bp at 2.50-, 3.00-, and 3.25-angstrom resolution, respectively. The highest-resolution structure shows fine details of specific protein-DNA interactions. The lower-resolution structures with longer DNA duplexes have similar interaction patterns and show how the flap domains interact with DNA in a sequence nonspecific fashion. Fifteen of 15 protein-DNA contacts predicted on the basis of the structure were confirmed by single amino acid mutations that abolished binding in vitro and complementation in vivo. A striking feature of the structure is the association of glutamate 71 from each subunit of the HetR dimer with three successive cytosines in each arm of the palindromic target, a feature that is conserved among all known heterocyst-forming cyanobacteria sequenced to date.; HetR is an essential regulator of heterocyst development in cyanobacteria. Many mutations in HetR render Anabaena incapable of nitrogen fixation. The protein binds to a DNA palindrome upstream of hetP and other genes. We have determined the crystal structures of HetR complexed with palindromic DNA targets, 21, 23, and 29 bp at 2.50-, 3.00-, and 3.25-angstrom resolution, respectively. The highest-resolution structure shows fine details of specific protein-DNA interactions. The lower-resolution structures with longer DNA duplexes have similar interaction patterns and show how the flap domains interact with DNA in a sequence nonspecific fashion. Fifteen of 15 protein-DNA contacts predicted on the basis of the structure were confirmed by single amino acid mutations that abolished binding in vitro and complementation in vivo. A striking feature of the structure is the association of glutamate 71 from each subunit of the HetR dimer with three successive cytosines in each arm of the palindromic target, a feature that is conserved among all known heterocyst-forming cyanobacteria sequenced to date.
SubtypeArticle
KeywordHeterocyst Differentiation Mutagenesis X-ray Crystallography
Department[Kim, Youngchang ; Joachimiak, Grazyna ; Joachimiak, Andrzej] Argonne Natl Lab, Midwest Ctr Struct Genom, Argonne, IL 60439 USA ; [Kim, Youngchang ; Joachimiak, Grazyna ; Joachimiak, Andrzej] Argonne Natl Lab, Struct Biol Ctr, Argonne, IL 60439 USA ; [Ye, Zi ; Zhao, Jindong] Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China ; [Videau, Patrick ; Young, Jasmine ; Hurd, Kathryn ; Callahan, Sean M.] Univ Hawaii, Dept Microbiol, Honolulu, HI 96822 USA ; [Gornicki, Piotr ; Haselkorn, Robert] Univ Chicago, Dept Mol Genet & Cell Biol, Chicago, IL 60637 USA ; [Joachimiak, Andrzej] Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA
DOI10.1073/pnas.1305971110
WOS HeadingsScience & Technology
Funding OrganizationNational Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357]
Indexed BySCI
Language英语
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000319327700004
WOS KeywordSTRAIN PCC 7120 ; HETEROCYST PATTERN-FORMATION ; REPRESSOR-OPERATOR COMPLEX ; CRYSTAL-STRUCTURE ; AMINO-ACIDS ; SP PCC-7120 ; RECOGNITION ; PROTEIN ; DIFFERENTIATION ; BINDING
Funding OrganizationNational Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357] ; National Institutes of Health [GM094585]; National Science Foundation [MCB-1121346]; Ellison Medical Foundation; US Department of Energy, Office of Biological and Environmental Research [DE-AC02-06CH11357]; US Department of Energy Office of Science laboratory [DE-AC02-06CH11357]
Citation statistics
Cited Times:18[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/19337
Collection水生生物分子与细胞生物学研究中心_期刊论文
Corresponding AuthorHaselkorn, R (reprint author), Univ Chicago, Dept Mol Genet & Cell Biol, 920 E 58Th St, Chicago, IL 60637 USA.
Affiliation1.Argonne Natl Lab, Midwest Ctr Struct Genom, Argonne, IL 60439 USA
2.Argonne Natl Lab, Struct Biol Ctr, Argonne, IL 60439 USA
3.Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Hubei, Peoples R China
4.Univ Hawaii, Dept Microbiol, Honolulu, HI 96822 USA
5.Univ Chicago, Dept Mol Genet & Cell Biol, Chicago, IL 60637 USA
6.Univ Chicago, Dept Biochem & Mol Biol, Chicago, IL 60637 USA
Recommended Citation
GB/T 7714
Kim, Youngchang,Ye, Zi,Joachimiak, Grazyna,et al. Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets[J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,2013,110(19):E1716-E1723.
APA Kim, Youngchang.,Ye, Zi.,Joachimiak, Grazyna.,Videau, Patrick.,Young, Jasmine.,...&Haselkorn, R .(2013).Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets.PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA,110(19),E1716-E1723.
MLA Kim, Youngchang,et al."Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets".PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 110.19(2013):E1716-E1723.
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