scholarly journals Binding of Euplotes octocarinatus centrin to peptide from xeroderma pigmentosum group C protein (XPC)

RSC Advances ◽  
2017 ◽  
Vol 7 (44) ◽  
pp. 27139-27149 ◽  
Author(s):  
Enxian Shi ◽  
Wenlong Zhang ◽  
Yaqin Zhao ◽  
Binsheng Yang
Keyword(s):  
Xeroderma Pigmentosum ◽  
C Protein ◽  
Hydrophobic Cavity ◽  
Α Helix ◽  
Euplotes Octocarinatus

Trp is buried in the hydrophobic cavity, the peptide folds into an α-helix, and the interaction is enthalpically driven from ITC.

scholarly journals The landscape of cytokinin binding by a plant nodulin

2013 ◽  
Vol 69 (12) ◽  
pp. 2365-2380 ◽  
Author(s):  
M. Ruszkowski ◽  
K. Szpotkowski ◽  
M. Sikorski ◽  
M. Jaskolski
Keyword(s):  
Root Nodules ◽  
Outer Cortex ◽  
Plant Host ◽  
Symbiotic Interaction ◽  
Model Legume ◽  
Hydrophobic Cavity ◽  
Density Maps ◽  
Loop Element ◽  
Α Helix ◽  
Related Proteins

Nodulation is an extraordinary symbiotic interaction between leguminous plants and nitrogen-fixing bacteria (rhizobia) that assimilate atmospheric nitrogen (in root nodules) and convert it into compounds suitable for the plant host. A class of plant hormones called cytokinins are involved in the nodulation process. In the model legumeMedicago truncatula, nodulin 13 (MtN13), which belongs to the pathogenesis-related proteins of class 10 (PR-10), is expressed in the outer cortex of the nodules. In general, PR-10 proteins are small and monomeric and have a characteristic fold with an internal hydrophobic cavity formed between a seven-stranded antiparallel β-sheet and a C-terminal α-helix. Previously, some PR-10 proteins not related to nodulation were found to bind cytokinins such astrans-zeatin. Here, four crystal structures of the MtN13 protein are reported in complexes with several cytokinins, namelytrans-zeatin,N6-isopentenyladenine, kinetin andN6-benzyladenine. All four phytohormones are bound in the hydrophobic cavity in the same manner and have excellent definition in the electron-density maps. The binding of the cytokinins appears to be strong and specific and is reinforced by several hydrogen bonds. Although the binding stoichiometry is 1:1, the complex is actually dimeric, with a cytokinin molecule bound in each subunit. The ligand-binding site in each cavity is formed with the participation of a loop element from the other subunit, which plugs the only entrance to the cavity. Interestingly, a homodimer of MtN13 is also formed in solution, as confirmed by small-angle X-ray scattering (SAXS).

scholarly journals The Xeroderma Pigmentosum Group C Protein Complex XPC-HR23B Plays an Important Role in the Recruitment of Transcription Factor IIH to Damaged DNA

2000 ◽  
Vol 275 (13) ◽  
pp. 9870-9875 ◽  
Author(s):  
Masayuki Yokoi ◽  
Chikahide Masutani ◽  
Takafumi Maekawa ◽  
Kaoru Sugasawa ◽  
Yoshiaki Ohkuma ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Protein Complex ◽  
Xeroderma Pigmentosum ◽  
C Protein ◽  
Damaged Dna

Structural, Thermodynamic, and Cellular Characterization of Human Centrin 2 Interaction with Xeroderma Pigmentosum Group C Protein

2007 ◽  
Vol 373 (4) ◽  
pp. 1032-1046 ◽  
Author(s):  
Jean-Baptiste Charbonnier ◽  
Emilie Renaud ◽  
Simona Miron ◽  
Marie Hélène Le Du ◽  
Yves Blouquit ◽  
...  
Keyword(s):  
Xeroderma Pigmentosum ◽  
C Protein

Flexibility and Plasticity of Human Centrin 2 Binding to the Xeroderma Pigmentosum Group C Protein (XPC) from Nuclear Excision Repair†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (11) ◽  
pp. 3653-3663 ◽  
Author(s):  
Ao Yang ◽  
Simona Miron ◽  
Liliane Mouawad ◽  
Patricia Duchambon ◽  
Yves Blouquit ◽  
...  
Keyword(s):  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
C Protein

scholarly journals Dynamic two-stage mechanism of versatile DNA damage recognition by xeroderma pigmentosum group C protein

2010 ◽  
Vol 685 (1-2) ◽  
pp. 21-28 ◽  
Author(s):  
Flurina C. Clement ◽  
Ulrike Camenisch ◽  
Jia Fei ◽  
Nina Kaczmarek ◽  
Nadine Mathieu ◽  
...  
Keyword(s):  
Dna Damage ◽  
Xeroderma Pigmentosum ◽  
Two Stage ◽  
C Protein ◽  
Damage Recognition ◽  
Dna Damage Recognition

scholarly journals Centrin 2 Stimulates Nucleotide Excision Repair by Interacting with Xeroderma Pigmentosum Group C Protein

2005 ◽  
Vol 25 (13) ◽  
pp. 5664-5674 ◽  
Author(s):  
Ryotaro Nishi ◽  
Yuki Okuda ◽  
Eriko Watanabe ◽  
Toshio Mori ◽  
Shigenori Iwai ◽  
...  
Keyword(s):  
Nucleotide Excision Repair ◽  
Xeroderma Pigmentosum ◽  
Excision Repair ◽  
Physical Interaction ◽  
C Protein ◽  
Damage Recognition ◽  
C Terminus ◽  
Nucleotide Excision ◽  
Dna Damage Recognition

ABSTRACT Xeroderma pigmentosum group C (XPC) protein plays a key role in DNA damage recognition in global genome nucleotide excision repair (NER). The protein forms in vivo a heterotrimeric complex involving one of the two human homologs of Saccharomyces cerevisiae Rad23p and centrin 2, a centrosomal protein. Because centrin 2 is dispensable for the cell-free NER reaction, its role in NER has been unclear. Binding experiments with a series of truncated XPC proteins allowed the centrin 2 binding domain to be mapped to a presumed α-helical region near the C terminus, and three amino acid substitutions in this domain abrogated interaction with centrin 2. Human cell lines stably expressing the mutant XPC protein exhibited a significant reduction in global genome NER activity. Furthermore, centrin 2 enhanced the cell-free NER dual incision and damaged DNA binding activities of XPC, which likely require physical interaction between XPC and centrin 2. These results reveal a novel vital function for centrin 2 in NER, the potentiation of damage recognition by XPC.

scholarly journals Targeting of the Sendai Virus C Protein to the Plasma Membrane via a Peptide-Only Membrane Anchor

2007 ◽  
Vol 81 (7) ◽  
pp. 3187-3197 ◽  
Author(s):  
Jean-Baptiste Marq ◽  
Albert Brini ◽  
Daniel Kolakofsky ◽  
Dominique Garcin
Keyword(s):  
Plasma Membrane ◽  
Sendai Virus ◽  
Intracellular Localization ◽  
Membrane Targeting ◽  
Membrane Anchor ◽  
C Protein ◽  
Cellular Antiviral Response ◽  
Α Helix ◽  
Virus C ◽  
Cellular Compartments

ABSTRACT Several cellular proteins are synthesized in the cytosol on free ribosomes and then associate with membranes due to the presence of short peptide sequences. These membrane-targeting sequences contain sites to which lipid chains are attached, which help direct the protein to a particular membrane domain and anchor it firmly in the bilayer. The intracellular concentration of these proteins in particular cellular compartments, where their interacting partners are also concentrated, is essential to their function. This paper reports that the apparently unmodified N-terminal sequence of the Sendai virus C protein (MPSFL KK IL K L R G RR . . .; letters in italics represent hydrophobic residues; underlined letters represent basic residues, which has a strong propensity to form an amphipathic α-helix in a hydrophobic environment) also function as a membrane targeting signal and membrane anchor. Moreover, the intracellular localization of the C protein at the plasma membrane is essential for inducing the interferon-independent phosphorylation of Stat1 as part of the viral program to prevent the cellular antiviral response.

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