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Furuta, A.

Publications and source records attributed to Furuta, A..

3 recordsLinked to original sources

Concomitant DNA hydroxymethylation and histone H2B O-GlcNAcylation are prerequisites for zygotic genome activation in mice

The paternal chromatin undergoes extensive reprogramming, characterized by the loss of 5-methylcytosine (5mC) through Ten-eleven translocation 3 (Tet3)-mediated oxidation to 5-hydroxymethylcytosine (5hmC). Given the role of DNA methylation in gene silencing, it has long been posited that this loss of paternal DNA methylation facilitates zygotic genome activation (ZGA), which occurs predominantly on the paternal genome. However, recent evidence indicates that Tet3-mediated 5mC oxidation alone does not influence global transcription in zygotes, leaving the molecular mechanisms governing ZGA largely elusive. Here, we identify the functional significance of O-linked N-acetylglucosamine (O-GlcNAc) modification of histone H2B at Serine 112 (H2BS112GlcNAc), catalyzed by O-GlcNAc transferase (OGT), within the paternal chromatin of mouse zygotes. We demonstrate that OGT is selectively recruited to the paternal chromatin because Stella (also known as PGC7 or Dppa3) inhibits its binding to the maternal chromatin--a recruitment mechanism analogous to that of Tet3. Although Tet3 and OGT associate with the paternal chromatin independently, both Tet3-dependent 5hmC formation and OGT-mediated H2BS112GlcNAcylation are indispensable for successful ZGA. Together, our findings reveal that a dual epigenetic signature--the simultaneous coordination of DNA hydroxymethylation and histone O-GlcNAcylation by Tet3 and OGT--is essential for initiating transcriptional reprogramming during the maternal-to-zygotic transition.

developmental biology↗

Structural snapshots of V/A-ATPase reveal a new paradigm for rotary catalysis

V/A-ATPase is a motor protein that shares a common rotary catalytic mechanism with FoF1 ATP synthase. When powered by ATP hydrolysis, the V1 moiety rotates the central rotor against the A3B3 hexamer, composed of three catalytic AB dimers adopting different conformations (ABopen, ABsemi, and ABclosed). Here we have determined the atomic models of 18 catalytic intermediates of the V1 moiety of V/A-ATPase under different reaction conditions by single particle Cryo-EM, which revealed that the rotor does not rotate immediately after binding of ATP to the V1. Instead, three events proceed simultaneously with the 120{degrees} rotation of the shaft: hydrolysis of ATP in ABsemi, zipper movement in ABopen by the binding ATP, and unzipper movement in ABclosed with release of both ADP and Pi. This indicates the unidirectional rotation of V/A-ATPase by a ratchet-like mechanism owing to ATP hydrolysis in ABsemi, rather than the power stroke model proposed previously for F1-ATPase.

biophysics↗

The mechanical inhibition of the isolated Vo from V-ATPase for proton conductance

V-ATPase is an energy converting enzyme, coupling ATP hydrolysis/synthesis in the hydrophilic V1 moiety, with proton flow through the Vo membrane moiety, via rotation of the central rotor complex relative to the surrounding stator apparatus. Upon dissociation from the V1 domain, the Vo of eukaryotic V-ATPase can adopt a physiologically relevant auto-inhibited form in which proton conductance through the Vo is prevented, however the molecular mechanism of this inhibition is not fully understood. Using cryo-electron microscopy, we determined the structure of both the holo V/A-ATPase and the isolated Vo at near-atomic resolution, respectively. These structures clarify how the isolated Vo adopts the auto-inhibited form and how the holo complex prevents the formation of this inhibited Vo form. One Sentence SummaryCryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H+ translocation in the Vo membrane domain.

biophysics↗