Akademska digitalna zbirka SLovenije - logo
E-viri
Celotno besedilo
Recenzirano
  • The linker histone Hho1 mod...
    Amigo, Roberto; Farkas, Carlos; Gidi, Cristian; Hepp, Matias I.; Cartes, Natalia; Tarifeño, Estefanía; Workman, Jerry L.; Gutiérrez, José L.

    Biochimica et biophysica acta. Gene regulatory mechanisms, January 2022, 2022-01-00, 20220101, Letnik: 1865, Številka: 1
    Journal Article

    Diverse factors play roles in chromatin dynamics, including linker proteins. Among them are high mobility group (HMG) box family proteins and linker histones. In the yeast Saccharomyces cerevisiae, Hmo1 has been identified as an HMG-box protein. This protein displays properties that are in agreement with this allocation. However, a number of studies have postulated that Hmo1 functions as a linker histone in yeast. On the other hand, when discovered, the Hho1 protein was identified as a linker histone. While multiple studies support this classification, some findings point to characteristics of Hho1 that are dissimilar to those commonly assigned to linker histones. In order to better understand the roles played by Hmo1 and Hho1 in chromatin dynamics and transcriptional regulation, we performed several analyses directly comparing these two proteins. Our analyses of genome-wide binding profiles support the belonging of Hmo1 to the HMGB family and Hho1 to the linker histones family. Interestingly, by performing protein-protein interaction analyses we found that both Hmo1 and Hho1 display physical interaction with the ATP-dependent chromatin remodeling complexes RSC, ISW1a and SWI/SNF. Moreover, by carrying out nucleosome remodeling assays, we found that both proteins stimulate the activity of the ISW1a complex. However, in the case of RSC, Hmo1 and Hho1 displayed differential properties, with Hho1 mainly showing an inhibitory effect. Our results are in agreement with the opposite roles played by RSC and ISW1a in chromatin dynamics and transcriptional regulation, and expand the view for the roles played by Hho1 and linker histones. •New properties found for Hmo1 are consistent with those present in HMG proteins.•Hho1 physically interacts with the nucleosome remodeling complexes RSC and ISW1a.•Hho1 stimulates ATP-dependent nucleosome remodeling activity of the ISW1a complex.•Hho1 exerts a differential effect on RSC and ISW1a remodeling activities.•The properties displayed by Hmo1 and Hho1 point to opposite or different roles.