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https://www.readbyqxmd.com/read/24070609/crystal-structure-of-pseudomonas-aeruginosa-transcriptional-regulator-pa2196-bound-to-its-operator-dna
#1
Yongwoon Kim, Yoora Kang, Jungwoo Choe
Pseudomonas aeruginosa is a major opportunistic human pathogen. PA2196 from P. aeruginosa is a member of TetR family of transcriptional repressors, which is involved in adaptation to environmental changes as well as bacterial antibiotic resistance. PA2196 consists of nine α-helical bundles divided into two separate domains. The N-terminal domain, called the DNA-binding domain, is composed of helices α1-α3 and has a helix-turn-helix motif. The C-terminal domain, called the ligand-binding domain, has a hydrophobic pocket for ligand binding...
October 18, 2013: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/22450759/thermodynamic-characterization-of-the-saccharomyces-cerevisiae-telomerase-rna-pseudoknot-domain-in-vitro
#2
Fei Liu, Yoora Kim, Charmion Cruickshank, Carla A Theimer
Recent structural and functional characterization of the pseudoknot in the Saccharomyces cerevisiae telomerase RNA (TLC1) has demonstrated that tertiary structure is present, similar to that previously described for the human and Kluyveromyces lactis telomerase RNAs. In order to biophysically characterize the identified pseudoknot secondary and tertiary structures, UV-monitored thermal denaturation experiments, nuclear magnetic resonance spectroscopy, and native gel electrophoresis were used to investigate various potential conformations in the pseudoknot domain in vitro, in the absence of the telomerase protein...
May 2012: RNA
https://www.readbyqxmd.com/read/21635871/crystal-structure-of-pseudomonas-aeruginosa-pa2196-a-putative-tetr-family-transcriptional-repressor
#3
Yoora Kang, Jungwoo Choe
PA2196 of Pseudomonas aeruginosa is a putative transcriptional regulator and belongs to the TetR family repressor that is involved in adaptations to environmental changes and bacterial antibiotic resistance. The crystal structure of PA2196 determined to 2.4Å resolution revealed nine α-helical bundles that can be divided into N-terminal DNA binding domain with an α-helix-turn-α-helix motif and C-terminal ligand binding domain with a hydrophobic ligand binding pocket. The distance between the N-terminal domains of homodimeric PA2196 suggested that our structure is similar to the DNA-bound form of other TetR family proteins...
June 24, 2011: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/18319618/hs-1-associated-protein-x-1-is-cleaved-by-caspase-3-during-apoptosis
#4
Ah Young Lee, Yoora Lee, Yun Kyung Park, Kwang-Hee Bae, Sayeon Cho, Do Hee Lee, Byoung Chul Park, Sunghyun Kang, Sung Goo Park
Caspase-3 (CASP3) plays a key role in apoptosis. In this study, HAX-1 was identified as a new substrate of CASP3 during apoptosis. HAX-1 was cleaved by CASP3 during etoposide-(ETO) induced apoptosis, and this event was inhibited by a CASP3-specific inhibitor. The cleavage site of HAX-1, at Asp(127), was located using N-terminal amino acid sequencing of in vitro cleavage products of recombinant HAX-1. Overexpression of HAX-1 inhibited ETO-induced apoptotic cell death. It also inhibited CASP3 activity. Together, these results suggest that HAX-1, a substrate of CASP3, inhibits the apoptotic process by inhibiting CASP3 activity...
February 29, 2008: Molecules and Cells
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