Molecular Characterization of HOXA2 and HOXA3 Binding Properties
The highly conserved HOX homeodomain (HD) transcription factors (TFs) establish the identity of different body parts along the antero–posterior axis of bilaterian animals. Segment diversification and the morphogenesis of different structures is achieved by generating precise patterns of HOX expressi...
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| Format: | Article |
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MDPI AG
2021-12-01
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| Series: | Journal of Developmental Biology |
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| Online Access: | https://www.mdpi.com/2221-3759/9/4/55 |
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| author | Joshua Mallen Manisha Kalsan Peyman Zarrineh Laure Bridoux Shandar Ahmad Nicoletta Bobola |
| author_facet | Joshua Mallen Manisha Kalsan Peyman Zarrineh Laure Bridoux Shandar Ahmad Nicoletta Bobola |
| author_sort | Joshua Mallen |
| collection | DOAJ |
| description | The highly conserved HOX homeodomain (HD) transcription factors (TFs) establish the identity of different body parts along the antero–posterior axis of bilaterian animals. Segment diversification and the morphogenesis of different structures is achieved by generating precise patterns of HOX expression along the antero–posterior axis and by the ability of different HOX TFs to instruct unique and specific transcriptional programs. However, HOX binding properties in vitro, characterised by the recognition of similar AT-rich binding sequences, do not account for the ability of different HOX to instruct segment-specific transcriptional programs. To address this problem, we previously compared HOXA2 and HOXA3 binding in vivo. Here, we explore if sequence motif enrichments observed in vivo are explained by binding affinities in vitro. Unexpectedly, we found that the highest enriched motif in HOXA2 peaks was not recognised by HOXA2 in vitro, highlighting the importance of investigating HOX binding in its physiological context. We also report the ability of HOXA2 and HOXA3 to heterodimerise, which may have functional consequences for the HOX patterning function in vivo. |
| first_indexed | 2024-03-10T03:50:16Z |
| format | Article |
| id | doaj.art-f117748cb7784d18b8066d41e764ad9a |
| institution | Directory Open Access Journal |
| issn | 2221-3759 |
| language | English |
| last_indexed | 2024-03-10T03:50:16Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Journal of Developmental Biology |
| spelling | doaj.art-f117748cb7784d18b8066d41e764ad9a2023-11-23T08:59:42ZengMDPI AGJournal of Developmental Biology2221-37592021-12-01945510.3390/jdb9040055Molecular Characterization of HOXA2 and HOXA3 Binding PropertiesJoshua Mallen0Manisha Kalsan1Peyman Zarrineh2Laure Bridoux3Shandar Ahmad4Nicoletta Bobola5School of Medical Sciences, University of Manchester, Manchester M13 9PT, UKSchool of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi 110067, IndiaSchool of Medical Sciences, University of Manchester, Manchester M13 9PT, UKLouvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, 5 (L7.07.10) Place Croix du Sud, 1348 Louvain-la-Neuve, BelgiumSchool of Computational and Integrative Sciences, Jawaharlal Nehru University, New Delhi 110067, IndiaSchool of Medical Sciences, University of Manchester, Manchester M13 9PT, UKThe highly conserved HOX homeodomain (HD) transcription factors (TFs) establish the identity of different body parts along the antero–posterior axis of bilaterian animals. Segment diversification and the morphogenesis of different structures is achieved by generating precise patterns of HOX expression along the antero–posterior axis and by the ability of different HOX TFs to instruct unique and specific transcriptional programs. However, HOX binding properties in vitro, characterised by the recognition of similar AT-rich binding sequences, do not account for the ability of different HOX to instruct segment-specific transcriptional programs. To address this problem, we previously compared HOXA2 and HOXA3 binding in vivo. Here, we explore if sequence motif enrichments observed in vivo are explained by binding affinities in vitro. Unexpectedly, we found that the highest enriched motif in HOXA2 peaks was not recognised by HOXA2 in vitro, highlighting the importance of investigating HOX binding in its physiological context. We also report the ability of HOXA2 and HOXA3 to heterodimerise, which may have functional consequences for the HOX patterning function in vivo.https://www.mdpi.com/2221-3759/9/4/55transcription factorHOXdevelopmentbranchial arches |
| spellingShingle | Joshua Mallen Manisha Kalsan Peyman Zarrineh Laure Bridoux Shandar Ahmad Nicoletta Bobola Molecular Characterization of HOXA2 and HOXA3 Binding Properties Journal of Developmental Biology transcription factor HOX development branchial arches |
| title | Molecular Characterization of HOXA2 and HOXA3 Binding Properties |
| title_full | Molecular Characterization of HOXA2 and HOXA3 Binding Properties |
| title_fullStr | Molecular Characterization of HOXA2 and HOXA3 Binding Properties |
| title_full_unstemmed | Molecular Characterization of HOXA2 and HOXA3 Binding Properties |
| title_short | Molecular Characterization of HOXA2 and HOXA3 Binding Properties |
| title_sort | molecular characterization of hoxa2 and hoxa3 binding properties |
| topic | transcription factor HOX development branchial arches |
| url | https://www.mdpi.com/2221-3759/9/4/55 |
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