Muryam A. Gourdet
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Muryam A. Gourdet has a total of 9 co-authors. Here are the top co-authors by number of shared publications:
- Elise N. Muñoz
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA 94158, USA
2 shared publications - Hao Wu
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, CA, USA
2 shared publications - Laura J. Hsieh
Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, USA
2 shared publications Cheng Yc
1 shared publicationChio Usc
1 shared publication- Geeta J. Narlikar
Department of Biochemistry and Biophysics, University of California at San Francisco
1 shared publication
Latest Publications
- Open Access
- 12 February 2026
- Published by EMBL-EBI
Single particle cryo-electron microscopy of the INO80-hexasome complex
- 12 February 2026
- Published by EMBL-EBI
Open AccessSingle particle cryo-electron microscopy of the INO80-hexasome complex
- Open Access
- 21 July 2023
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 381 (6655) , 319-324
Reorientation of INO80 on hexasomes reveals basis for mechanistic versatility
Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of Saccharomyces cerevisiae INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location –2 (SHL –2), in contrast to SHL –6 and SHL –7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL –2. The SHL –2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles.
- 21 July 2023
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 381 (6655) , 319-324
Open AccessReorientation of INO80 on hexasomes reveals basis for mechanistic versatility
Unlike other chromatin remodelers, INO80 preferentially mobilizes hexasomes, which can form during transcription. Why INO80 prefers hexasomes over nucleosomes remains unclear. Here, we report structures of Saccharomyces cerevisiae INO80 bound to a hexasome or a nucleosome. INO80 binds the two substrates in substantially different orientations. On a hexasome, INO80 places its ATPase subunit, Ino80, at superhelical location –2 (SHL –2), in contrast to SHL –6 and SHL –7, as previously seen on nucleosomes. Our results suggest that INO80 action on hexasomes resembles action by other remodelers on nucleosomes such that Ino80 is maximally active near SHL –2. The SHL –2 position also plays a critical role for nucleosome remodeling by INO80. Overall, the mechanistic adaptations used by INO80 for preferential hexasome sliding imply that subnucleosomal particles play considerable regulatory roles.