codon-optimized open reading frame for human dss1 Search Results


codon-optimized open reading frame for human dss1  (GenScript corporation)
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GenScript corporation codon-optimized open reading frame for human dss1
HDX changes between RPA and RPA S384D are shown in the ( a ) absence or ( b ) presence of ssDNA (ssDNA is depicted in black). Changes in deuterium incorporation are observed in almost all DNA binding and protein-interaction domains. Data are mapped onto the structure of human RPA which is built using the structures of the OB domains from crystal structures. The regions colored yellow correspond to peptides that were not identified in the MS analysis of either or both the wild type and mutant RPA samples. The flexible linkers were modeled using AlphaFold. The position of Ser-384 is denoted in green. Data are presented as ±SDM from three independent experiments. Bio-layer interferometry analysis of RPA or RPA S384D binding to <t>DSS1</t> in the ( c ) absence or ( d ) presence of ssDNA. RPA S384D shows reduced binding to DSS1 in the absence of DNA. When ssDNA-bound, almost complete loss of DSS1 binding to RPA is observed.
Codon Optimized Open Reading Frame For Human Dss1, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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codon-optimized open reading frame for human dss1 - by Bioz Stars, 2026-05
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HDX changes between RPA and RPA S384D are shown in the ( a ) absence or ( b ) presence of ssDNA (ssDNA is depicted in black). Changes in deuterium incorporation are observed in almost all DNA binding and protein-interaction domains. Data are mapped onto the structure of human RPA which is built using the structures of the OB domains from crystal structures. The regions colored yellow correspond to peptides that were not identified in the MS analysis of either or both the wild type and mutant RPA samples. The flexible linkers were modeled using AlphaFold. The position of Ser-384 is denoted in green. Data are presented as ±SDM from three independent experiments. Bio-layer interferometry analysis of RPA or RPA S384D binding to DSS1 in the ( c ) absence or ( d ) presence of ssDNA. RPA S384D shows reduced binding to DSS1 in the absence of DNA. When ssDNA-bound, almost complete loss of DSS1 binding to RPA is observed.

Journal: Nature Communications

Article Title: An Aurora B-RPA signaling axis secures chromosome segregation fidelity

doi: 10.1038/s41467-023-38711-2

Figure Lengend Snippet: HDX changes between RPA and RPA S384D are shown in the ( a ) absence or ( b ) presence of ssDNA (ssDNA is depicted in black). Changes in deuterium incorporation are observed in almost all DNA binding and protein-interaction domains. Data are mapped onto the structure of human RPA which is built using the structures of the OB domains from crystal structures. The regions colored yellow correspond to peptides that were not identified in the MS analysis of either or both the wild type and mutant RPA samples. The flexible linkers were modeled using AlphaFold. The position of Ser-384 is denoted in green. Data are presented as ±SDM from three independent experiments. Bio-layer interferometry analysis of RPA or RPA S384D binding to DSS1 in the ( c ) absence or ( d ) presence of ssDNA. RPA S384D shows reduced binding to DSS1 in the absence of DNA. When ssDNA-bound, almost complete loss of DSS1 binding to RPA is observed.

Article Snippet: A codon-optimized open reading frame for Human DSS1 (DSS1) was synthesized (Genscript Inc.) with a SUMO protease cleavable N-terminal MVKIH-Strep-6x-HIS-SUMO tag.

Techniques: Binding Assay, Mutagenesis

During mitosis, RPA bound to ssDNA intermediates or free in solution is phosphorylated by Aurora B kinase at Ser-384 (DBD-B) in the large RPA70 subunit. We propose that phosphorylation releases the protein-interaction domains (OB-F or PID 70N and wh or PID 32C ) and promotes the formation of higher-density RPA-bound ssDNA filaments. The protein-interaction domains can then promote binding to RPA-interacting proteins. The feedback mechanism that modulates Aurora B activity through RPA phosphorylation and the involvement of R loops also remains to be elucidated. Since the site of phosphorylation resides close to the DSS1 binding site, recruitment of DSS1-BRCA2 is inhibited leading to suppression of homologous recombination during mitosis. Deregulation of the Aurora B-RPA signaling circuit leads to errors in chromosome segregation fidelity.

Journal: Nature Communications

Article Title: An Aurora B-RPA signaling axis secures chromosome segregation fidelity

doi: 10.1038/s41467-023-38711-2

Figure Lengend Snippet: During mitosis, RPA bound to ssDNA intermediates or free in solution is phosphorylated by Aurora B kinase at Ser-384 (DBD-B) in the large RPA70 subunit. We propose that phosphorylation releases the protein-interaction domains (OB-F or PID 70N and wh or PID 32C ) and promotes the formation of higher-density RPA-bound ssDNA filaments. The protein-interaction domains can then promote binding to RPA-interacting proteins. The feedback mechanism that modulates Aurora B activity through RPA phosphorylation and the involvement of R loops also remains to be elucidated. Since the site of phosphorylation resides close to the DSS1 binding site, recruitment of DSS1-BRCA2 is inhibited leading to suppression of homologous recombination during mitosis. Deregulation of the Aurora B-RPA signaling circuit leads to errors in chromosome segregation fidelity.

Article Snippet: A codon-optimized open reading frame for Human DSS1 (DSS1) was synthesized (Genscript Inc.) with a SUMO protease cleavable N-terminal MVKIH-Strep-6x-HIS-SUMO tag.

Techniques: Phospho-proteomics, Binding Assay, Activity Assay, Homologous Recombination