Please use this identifier to cite or link to this item: http://223.31.159.10:8080/jspui/handle/123456789/1192
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dc.contributor.authorKumar, Amish-
dc.contributor.authorYadav, Gitanjali-
dc.date.accessioned2021-06-04T07:34:44Z-
dc.date.available2021-06-04T07:34:44Z-
dc.date.issued2021-
dc.identifier.citationJournal of Bioinformatics and Computational Biology, 19: 2140001en_US
dc.identifier.issn0219-7200-
dc.identifier.otherhttps://doi.org/10.1142/S0219720021400011-
dc.identifier.urihttps://www.worldscientific.com/doi/10.1142/S0219720021400011-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/1192-
dc.descriptionAccepted date: 23 December 2020en_US
dc.description.abstractThe three helical Histone Fold Motif (HFM) of core histone proteins provides an evolutionarily favored site for the protein–DNA interface. Despite significant variation in sequence, the HFM retains a distinctive structural fold that has diversified into several non-histone protein families. In this work, we explore the ancestry of non-histone HFM containing families in the plant kingdom. A sequence search algorithm was developed using iterative profile Hidden Markov Models to identify remote homologs of core-histone proteins. The resulting hits were functionally annotated, classified into families, and subjected to comprehensive phylogenetic analyses via Maximum likelihood and Bayesian methods. We have identified 4390 HFM containing proteins in the plant kingdom that are not histones, mostly existing as diverse transcription factor families, distributed widely within and across taxonomic groups. Patterns of homology suggest that core histone subunit H2A has evolved into newer families like NF-YC and DRAP1, whereas the H2B subunit of core histones shares a common ancestry with NF-YB and DR1 class of TFs. Core histone subunits H3 and H4 were found to have evolved into DPE and TAF proteins, respectively. Taken together these results provide insights into diversification events during the evolution of the HFM, including sub-functionalization and neo-functionalization of the HFM.en_US
dc.language.isoen_USen_US
dc.publisherWorld Scientific Publishing Co Pte Ltden_US
dc.subjectHistoneen_US
dc.subjectnon-histonesen_US
dc.subjectNF-Yen_US
dc.subjectTAFen_US
dc.subjectDRAP1en_US
dc.subjectCEN-Sen_US
dc.titleShared ancestry of core-histone subunits and non-histone plant proteins containing the Histone Fold Motif (HFM)en_US
dc.typeArticleen_US
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