The True Story of Yeti, the "Abominable" Heterochromatic Gene of Drosophila melanogaster.

Yuri Prozzillo,Stefano Cuticone,Giovanni Messina,Diego Ferreri,Patrizio Dimitri,Francesca Delle Monache

doi:10.3389/fphys.2019.01093

Yuri Prozzillo, Stefano Cuticone + Show 4 more

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https://doi.org/10.3389/fphys.2019.01093

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Abstract

The Drosophila Yeti gene (CG40218) was originally identified by recessive lethal mutation and subsequently mapped to the deep pericentromeric heterochromatin of chromosome 2. Functional studies have shown that Yeti encodes a 241 amino acid protein called YETI belonging to the evolutionarily conserved family of Bucentaur (BCNT) proteins and exhibiting a widespread distribution in animals and plants. Later studies have demonstrated that YETI protein: (i) is able to bind both subunits of the microtubule-based motor kinesin-I; (ii) is required for proper chromosome organization in both mitosis and meiosis divisions; and more recently (iii) is a new subunit of dTip60 chromatin remodeling complex. To date, other functions of YETI counterparts in chicken (CENtromere Protein 29, CENP-29), mouse (Cranio Protein 27, CP27), zebrafish and human (CranioFacial Development Protein 1, CFDP1) have been reported in literature, but the fully understanding of the multifaceted molecular function of this protein family remains still unclear. In this review we comprehensively highlight recent work and provide a more extensive hypothesis suggesting a broader range of YETI protein functions in different cellular processes.

Highlights

The eukaryotic genome is packaged into a highly condensed structure known as chromatin allowing cells to organize, compact and stabilize the genome into the nucleus
The BCNT domain of YETI was found to be involved in chromatin binding through the interaction with the H2A histone variant (H2A.V), Domino-A (DOM-A) ATPase, and HP1a protein (Ryu et al, 2014; Figure 3). These results strongly suggest that YETI may be directly implicated in the exchange of the variant H2A.V onto nucleosomes impacting on the dynamic changes of chromatin, and fulfilling its role as subunit of Tip60 chromatin remodeling complex, to the yeast homolog SWC5 (Morillo-Huesca et al, 2010)
Independent experimental evidence suggests that the human CRANIOFACIAL DEVELOPMENT PROTEIN 1 (CFDP1) protein is a subunit of the SNF2-related CBP activator protein (SRCAP) chromatin remodeling complex (Havugimana et al, 2012; Messina et al, 2017), which catalyzes the ATP-dependent replacement of canonical histone H2A with the H2A.Z variant (Monroy et al, 2001)

Summary

Introduction

The eukaryotic genome is packaged into a highly condensed structure known as chromatin allowing cells to organize, compact and stabilize the genome into the nucleus. The human (SRCAP and P400/Tip60) and Drosophila (dTip60) orthologous chromatin remodeling complexes include proteins with high similarity to the subunits of two distinct chromatin-modifying complexes, the yeast NuA4 complex (Wang et al, 2018) harboring HAT (Histone Acetyl-transferase) activity, and the SWR1 ATP-dependent chromatin remodeling complex which catalyzes histones exchange (Table 1).

Results

Conclusion