Arabidopsis HEAT SHOCK FACTOR BINDING PROTEIN is required to limit meiotic crossovers and HEI10 transcription

The number of meiotic crossovers is tightly controlled and most depend on pro-crossover ZMM proteins, such as the E3 ligase HEI10. Despite the importance of HEI10 dosage for crossover formation, how HEI10 transcription is controlled remains unexplored. In a forward genetic screen using a fluorescent crossover reporter in Arabidopsis thaliana, we identify heat shock factor binding protein (HSBP) as a repressor of HEI10 transcription and crossover numbers. Using genome-wide crossover mapping and cytogenetics, we show that hsbp mutations or meiotic HSBP knockdowns increase ZMM-dependent crossovers toward the telomeres, mirroring the effects of HEI10 overexpression. Through RNA sequencing, DNA methylome, and chromatin immunoprecipitation analysis, we reveal that HSBP is required to repress HEI10 transcription by binding with heat shock factors (HSFs) at the HEI10 promoter and maintaining DNA methylation over the HEI10 5′ untranslated region. Our findings provide insights into how the temperature response regulator HSBP restricts meiotic HEI10 transcription and crossover number by attenuating HSF activity.

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  • Name: Kim, Juhyun, Type: Corresponding Author,
  • Name: Park, Jihye, Type: Author,
  • Name: Kim, Heejin, Type: Author,
  • Name: Son, Namil, Type: Author,
  • Name: Kim, Eun‐Jung, Type: Author,
  • Name: Kim, Jaeil, Type: Author,
  • Name: Byun, Dohwan, Type: Author,
  • Name: Lee, Youngkyung, Type: Author,
  • Name: Park, Yeong Mi, Type: Author,
  • Name: Nageswaran, Divyashree C, Type: Author,
  • Name: Kuo, Pallas, Type: Author,
  • Name: Rose, Teresa, Type: Author,
  • Name: Dang, Tuong Vi T, Type: Author,
  • Name: Hwang, Ildoo, Type: Author,
  • Name: Lambing, Christophe, Type: Author,
  • Name: Henderson, Ian R, Type: Author,
  • Name: Choi, Kyuha, Type: Author,
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Citation Report https://scite.ai/reports/10.15252/embj.2021109958
DFW Organisation RRes
DFW Work Package 1
DOI 10.15252/embj.2021109958
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Open Access Status closed
Publisher URL https://www.embopress.org/doi/full/10.15252/embj.2021109958