Výsledky vyhledávání - "Ann E. Maris"

Structure and Properties of a Re-engineered Homeodomain Protein–DNA Interface

Autor: Daniel Rauh, Matthew D. Simon, Ann E. Maris, Kevan M. Shokat, David E. Wemmer, Morris E. Feldman

Publikováno v: ACS Chemical Biology. 1:755-760

The homeodomain (HD)-DNA interface has been conserved over 500 million years of evolution. Despite this conservation, we have successfully re-engineered the engrailed HD to specifically recognize an unnatural nucleotide using a phage display selectio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c993051d897ec29f6f0aa8eb616b1d28
https://doi.org/10.1021/cb6003756

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Negative Regulation of AAA+ ATPase Assembly by Two Component Receiver Domains: A Transcription Activation Mechanism that is Conserved in Mesophilic and Extremely Hyperthermophilic Bacteria

Autor: Baoyu Chen, Elena Kondrashkina, B. Tracy Nixon, Michaeleen Doucleff, David E. Wemmer, Ann E. Maris

Publikováno v: Journal of Molecular Biology. 353:242-255

Only a few transcriptional regulatory proteins have been characterized in extremely hyperthermophilic organisms, and most function as repressors. Structural features of the NtrC1 protein from the hyperthermophilic bacterium Aquifex aeolicus suggested

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c47b2fd1a6e12ac8bddb5b7438f1d4d6
https://doi.org/10.1016/j.jmb.2005.08.003

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Dimerization allows DNA target site recognition by the NarL response regulator

Autor: Mary L. Kopka, Shawn M D Bearson, Ann E. Maris, Richard E. Dickerson, Michael R. Sawaya, Michael Jarvis, Imke Schröder, Maria Kaczor-Grzeskowiak, Robert P. Gunsalus

Publikováno v: Nature Structural Biology. 9:771-778

Two-component signal transduction systems are modular phosphorelay regulatory pathways common in prokaryotes. In the co-crystal structure of the Escherichia coli NarL signal output domain bound to DNA, we observe how the NarL family of two-component

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e6e2e5b024f0cfbeebfeb9c2c6c49ab
https://doi.org/10.1038/nsb845

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Structure, function, and tethering of DNA-binding domains in σ54transcriptional activators

Autor: Anisa Young, Natasha K. Vidangos, Joseph D. Batchelor, Ann E. Maris, Eunmi Hong, David E. Wemmer, Jeffrey G. Pelton

Publikováno v: Vidangos, N; Maris, AE; Young, A; Hong, E; Pelton, JG; Batchelor, JD; et al.(2013). Structure, function, and tethering of DNA-binding domains in σ54transcriptional activators. Biopolymers, 99(12), 1082-1096. doi: 10.1002/bip.22333. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/4w25j1nc

We compare the structure, activity, and linkage of DNA-binding domains (DBDs) from σ54transcriptional activators and discuss how the properties of the DBDs and the linker to the neighboring domain are affected by the overall properties and requireme

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f0fc1aa03e1fc2f29db2704b7aaf8c6
https://doi.org/10.1002/bip.22333

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Structure, function, and tethering of DNA-binding domains in σ⁵⁴ transcriptional activators

Autor: Natasha, Vidangos, Ann E, Maris, Anisa, Young, Eunmi, Hong, Jeffrey G, Pelton, Joseph D, Batchelor, David E, Wemmer

Publikováno v: Biopolymers. 99(12)

We compare the structure, activity, and linkage of DNA-binding domains (DBDs) from σ(54) transcriptional activators and discuss how the properties of the DBDs and the linker to the neighboring domain are affected by the overall properties and requir

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d19d587c014a03e9be3a2a92afb21e03
https://pubmed.ncbi.nlm.nih.gov/23818155

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Primary and secondary modes of DNA recognition by the NarL two-component response regulator

Autor: Richard E. Dickerson, Robert P. Gunsalus, Ann E. Maris, Zhongcai Ma, Mary L. Kopka, Maria Kaczor-Grzeskowiak

Publikováno v: Biochemistry. 44(44)

NarL is a model response regulator for bacterial two-component signal transduction. The NarL C-terminal domain DNA binding domain alone (NarL(C)) contains all essential DNA binding determinants of the full-length NarL transcription factor. In the ful

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c770ec4d28f9268f064aaf06535968c
https://pubmed.ncbi.nlm.nih.gov/16262254

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The response regulator OmpR oligomerizes via beta-sheets to form head-to-head dimers

Autor: Nicole Byers, Don Walthers, Ann E. Maris, Kirsten Mattison, Linda J. Kenney

Publikováno v: Journal of molecular biology. 350(5)

In Escherichia coli, the EnvZ/OmpR two-component regulatory system regulates expression of the porin genes ompF and ompC in response to changes in osmolarity. It has recently become apparent that OmpR functions as a global regulator, by regulating th

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https://pubmed.ncbi.nlm.nih.gov/15979641

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The response regulator BvgA and RNA polymerase alpha subunit C-terminal domain bind simultaneously to different faces of the same segment of promoter DNA

Autor: Mei-Shin Yang, Ann E. Maris, Philip E. Boucher, Scott Stibitz

Publikováno v: Molecular cell. 11(1)

Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec6d96795eb66572e291a063ad131d8b
https://pubmed.ncbi.nlm.nih.gov/12535530

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