EMSA-SELEX-seq method for analysis of binding site sequences in DNA-protein complexes

封面

如何引用文章

全文:

开放存取 开放存取
受限制的访问 ##reader.subscriptionAccessGranted##
受限制的访问 订阅存取

详细

The BOB1 protein (OBF1, OCA-B) is a transcriptional coactivator of two POU domain proteins — OCT1, expressed in all cells, and lymphoid-specific OCT2. The interaction of BOB1 with OCT1/2 plays an important role in the regulation of immune responses in both physiological and pathological contexts. BOB1 is known to form a ternary complex with OCT1/2 bound to DNA in monomeric and certain dimeric configurations, changing the sequence specificity of the binding. To analyze DNA sequences from these complexes, in this work we proposed the EMSA-SELEX-seq method, based on the separation of OCT/BOB1 complexes of various compositions in a non-denaturing polyacrylamide gel (EMSA) followed by the isolation and amplification of the oligonucleotides that they contain (SELEX). Based on several rounds of the enrichment followed by the NGS sequencing and bioinformatics analysis, the DNA sequences were determined and the relevance of this approach was confirmed. Thus, the proposed EMSA-SELEX-seq method allows the analysis of DNA sequences in DNA-protein complexes with varying dimensions of its protein components.

作者简介

I. Nazarov

Institute of Cytology RAS

编辑信件的主要联系方式.
Email: i.nazarov@incras.ru
俄罗斯联邦, St. Petersburg, 194064

M. Gordeev

Institute of Cytology RAS

Email: i.nazarov@incras.ru
俄罗斯联邦, St. Petersburg, 194064

A. Kuzmin

Institute of Cytology RAS

Email: i.nazarov@incras.ru
俄罗斯联邦, St. Petersburg, 194064

D. Zilov

Institute of Cytology RAS

Email: i.nazarov@incras.ru
俄罗斯联邦, St. Petersburg, 194064

E. Potapenko

University of Haifa

Email: i.nazarov@incras.ru

Institute of Evolution, Department of Evolutionary and Environmental Biology

以色列, Haifa, 3498838

A. Tomilin

Institute of Cytology RAS

Email: a.tomilin@incras.ru
俄罗斯联邦, St. Petersburg, 194064

参考

  1. Bailey T. L., Elkan C. 1994. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. In: Proceedings of the Second International Conference on Intelligent Systems for Molecular Biology. Menlo Park, California: AAAI Press. P. 28.
  2. Botquin V., Hess H., Fuhrmann G., Anastassiadis C., Gross M. K., Vriend G., Schöler H. R. 1998. New POU dimer configuration mediates antagonistic control of an osteopontin preimplantation enhancer by Oct-4 and Sox-2. Genes Dev. V. 12. P. 2073.
  3. Gstaiger M., Georgiev O., van Leeuwen H., van der Vliet P., Schaffner W. 1996. The B cell coactivator Bob1 shows DNA sequence-dependent complex formation with Oct-1/Oct-2 factors, leading to differential promoter activation. EMBO J. V. 15. P. 2781.
  4. Gstaiger M., Knoepfel L., Georgiev O., Schaffner W., Hovens C. M. 1995. A B-cell coactivator of octamer-binding transcription factors. Nature. V. 373. P. 360.
  5. Jolma A., Yan J., Whitington T., Toivonen J., Nitta K. R., Rastas P., Morgunova E., Enge M., Taipale M., Wei G., Palin K., Vaquerizas J. M., Vincentelli R., Luscombe N. M., Hughes T. R., et al. 2013. DNA-binding specificities of human transcription factors. Cell. V. 152. P. 327.
  6. Jolma A., Yin Y., Nitta K. R., Dave K., Popov A., Taipale M., Enge M., Kivioja T., Morgunova E., Taipale J. 2015. DNA-dependent formation of transcription factor pairs alters their binding specificity. Nature. V. 527. P. 384.
  7. Kibet C. K., Machanick P. 2015. Transcription factor motif quality assessment requires systematic comparative analysis. F1000Res. V. 4: ISCB Comm J-1429.
  8. Luo Y., Fujii H., Gerster T., Roeder R. G. 1992. A novel B cell-derived coactivator potentiates the activation of immunoglobulin promoters by octamer-binding transcription factors. Cell. V. 71. P. 231.
  9. Luo Y., Roeder R. G. 1995. Cloning, functional characterization, and mechanism of action of the B-cell-specific transcriptional coactivator OCA-B. Mol. Cell Biol. V. 15. P. 4115.
  10. Meers M. P., Janssens D. H., Henikoff S. 2019. Pioneer factor-nucleosome binding events during differentiation are motif encoded. Mol. Cell. V. 75. P. 562.
  11. Reményi A., Tomilin A., Pohl E., Lins K., Philippsen A., Reinbold R., Schöler H. R., Wilmanns M. 2001. Differential dimer activities of the transcription factor Oct-1 by DNA-induced interface swapping. Mol. Cell. V. 8. P. 569.
  12. Song S., Cao C., Choukrallah M. A., Tang F., Christofori G., Kohler H., Wu F., Fodor B. D., Frederiksen M., Willis S. N., Jackson J. T., Nutt S. L., Dirnhofer S., Stadler M. B., Matthias P. 2021. OBF1 and Oct factors control the germinal center transcriptional program. Blood. V. 137. P. 2920.
  13. Strubin M., Newell J. W., Matthias P. 1995. OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin promoter activity through association with octamer-binding proteins. Cell. V. 80 P. 497.
  14. Tomilin A., Reményi A., Lins K., Bak H., Leidel S., Vriend G., Wilmanns M., Schöler H. R. 2000. Synergism with the coactivator OBF-1 (OCA-B, BOB-1) is mediated by a specific POU dimer configuration. Cell. V. 103. P. 853.
  15. Weirauch M. T., Cote A., Norel R., Annala M., Zhao Y., Riley T. R., Saez-Rodriguez J., Cokelaer T., Vedenko A., Talukder S., DREAM5 Consortium, Bussemaker H. J., Morris Q. D., Bulyk M. L., Stolovitzky G. et al. 2013. Evaluation of methods for modeling transcription factor sequence specificity. Nat. Biotechnol. V. 31. P. 126.

补充文件

附件文件
动作
1. JATS XML

版权所有 © Russian Academy of Sciences, 2024