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Cohesin SA1 and SA2 are RNA binding proteins that localize to RNA containing regions on DNA.
Pan, Hai; Jin, Miao; Ghadiyaram, Ashwin; Kaur, Parminder; Miller, Henry E; Ta, Hai Minh; Liu, Ming; Fan, Yanlin; Mahn, Chelsea; Gorthi, Aparna; You, Changjiang; Piehler, Jacob; Riehn, Robert; Bishop, Alexander J R; Tao, Yizhi Jane; Wang, Hong.
Afiliación
  • Pan H; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
  • Jin M; Department of BioSciences, Rice University, Houston, TX 77251, USA.
  • Ghadiyaram A; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
  • Kaur P; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
  • Miller HE; Center for Human Health and the Environment, North Carolina State University, Raleigh, NC 27695, USA.
  • Ta HM; Greehey Children's Cancer Research Institute, University of Texas Health at San Antonio, TX 78229, USA.
  • Liu M; Department of Cell Systems and Anatomy, University of Texas Health at San Antonio, TX 78229, USA.
  • Fan Y; Department of BioSciences, Rice University, Houston, TX 77251, USA.
  • Mahn C; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
  • Gorthi A; Department of BioSciences, Rice University, Houston, TX 77251, USA.
  • You C; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
  • Piehler J; Greehey Children's Cancer Research Institute, University of Texas Health at San Antonio, TX 78229, USA.
  • Riehn R; Department of Cell Systems and Anatomy, University of Texas Health at San Antonio, TX 78229, USA.
  • Bishop AJR; Division of Biophysics, Universität Osnabrück, Barbarstrasse 11, 49076 Osnabrück, Germany.
  • Tao YJ; Division of Biophysics, Universität Osnabrück, Barbarstrasse 11, 49076 Osnabrück, Germany.
  • Wang H; Physics Department, North Carolina State University, Raleigh, NC 27695, USA.
Nucleic Acids Res ; 48(10): 5639-5655, 2020 06 04.
Article en En | MEDLINE | ID: mdl-32352519
Cohesin SA1 (STAG1) and SA2 (STAG2) are key components of the cohesin complex. Previous studies have highlighted the unique contributions by SA1 and SA2 to 3D chromatin organization, DNA replication fork progression, and DNA double-strand break (DSB) repair. Recently, we discovered that cohesin SA1 and SA2 are DNA binding proteins. Given the recently discovered link between SA2 and RNA-mediated biological pathways, we investigated whether or not SA1 and SA2 directly bind to RNA using a combination of bulk biochemical assays and single-molecule techniques, including atomic force microscopy (AFM) and the DNA tightrope assay. We discovered that both SA1 and SA2 bind to various RNA containing substrates, including ssRNA, dsRNA, RNA:DNA hybrids, and R-loops. Importantly, both SA1 and SA2 localize to regions on dsDNA that contain RNA. We directly compared the SA1/SA2 binding and R-loops sites extracted from Chromatin Immunoprecipitation sequencing (ChIP-seq) and DNA-RNA Immunoprecipitation sequencing (DRIP-Seq) data sets, respectively. This analysis revealed that SA1 and SA2 binding sites overlap significantly with R-loops. The majority of R-loop-localized SA1 and SA2 are also sites where other subunits of the cohesin complex bind. These results provide a new direction for future investigation of the diverse biological functions of SA1 and SA2.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Cromosómicas no Histona / Proteínas de Unión al ARN / Proteínas de Ciclo Celular / Estructuras R-Loop Idioma: En Revista: Nucleic Acids Res Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Cromosómicas no Histona / Proteínas de Unión al ARN / Proteínas de Ciclo Celular / Estructuras R-Loop Idioma: En Revista: Nucleic Acids Res Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido