@Joyeechakra

Postdoctoral Associate @NIH, Postdoctoral Associate @BCMHouston @TXmedcenter, PhD @IISERPune. Structural biochemist.

 Bethesda, MD
Joined October 2022
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  • Followers278
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Delighted to share our work, recently published in @jbiolchem Check it out here- Dynamics of interdomain rotation facilitates FtsZ filament assembly - Journal of Biological Chemistry jbc.org/article/S0021-9258%2…

Dynamics of interdomain rotation facilitates FtsZ filament assembly

FtsZ, the tubulin homolog essential for bacterial cell division, assembles as the Z-ring at the division site, and directs peptidoglycan synthesis by treadmilling. It is unclear how FtsZ achieves...

jbc.org
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Soumyajit Dutta@soumyashuvroJul 8
The structural work of my PhD thesis is finally out now as a preprint in Biorxiv. 🤗 Here, we have used cryo-EM and molecular dynamics simulations to understand the basis of curvature in FtsZ protein filament. biorxiv.org/content/10.64898…

Lateral interactions override nucleotide state in determining FtsZ filament curvature

The bacterial tubulin homolog FtsZ assembles into dynamic filaments that form the cytokinetic Z-ring and drives constriction during cell division. Whether a nucleotide-dependent FtsZ filament...

biorxiv.org
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Dilip Kumar Tiwari@dkumar028 Oct 2025
Prof. BVV Prasad, a DST-VAIBHAV fellow, gave an engaging talk on the "molecular choreography of viral proteins" on the occasion of birth anniversary of a genius scientist Prof. G N Ramachandran. Thank you @Icosahedral16 lab for hosting. @iitdelhi @sathi_iitdelhi @TSB_Ashoka
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Soumyajit Dutta@soumyashuvro5 Apr 2025
Excited to share our Mycoplasma FtsZ work now published in Biochemistry @ACSPublications. Congratulations to all the authors @sakshipoddar20 @Joyeechakra @kuruhoornambi pubs.acs.org/doi/10.1021/acs… #Celldivision #Bacteria #FtsZ #Mycoplasma

Membrane Binding and Cholesterol Sensing Motif in Mycoplasma genitalium FtsZ: A Novel Mode of...

Abstract. Cell division in bacteria is initiated by constriction of the Z-ring comprising two essential proteins, FtsZ and FtsA. Though the essential funct

pubs.acs.org
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Krishnendu Roy@itskrishnendu319 Mar 2025
Happy to share a part of my PhD work in @TPucadyil lab now online @NatureComms. In collaboration with Joshua Pemberton and Tamas Balla, we show how local production of lipids on #mitochondrial surface regulates the activity of membrane shaping proteins. nature.com/articles/s41467-0…

Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochond...

Nature Communications - Using complementary live cell approaches together with a powerful in vitro reconstitution system, this study demonstrates the direct regulation of mitochondrial dynamics by...

nature.com
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Congratulations @itskrishnendu3 and all the authors 🎊
Cell Biology J-Club@cell_club19 Mar 2025
Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochondrial tubulation and fission nature.com/articles/s41467-0…

Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochond...

Nature Communications - Using complementary live cell approaches together with a powerful in vitro reconstitution system, this study demonstrates the direct regulation of mitochondrial dynamics by...

nature.com
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New online! Norovirus replication, host interactions and vaccine advances go.nature.com/4jnwOjh
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Drs. V Prasad, S Kaundal, @EstesLab_BCM et al have discovered replication hubs for #human #norovirus. @ScienceAdvances @bcmhouston #biomolecularCondensates #enteroids #PositiveRNAvirus @bcm_gihep @BCMCancerCenter @CPRITTexas bcm.edu/news/researchers-dis…

Researchers discovered replication hubs for human norovirus

Human norovirus, the leading cause of viral gastroenteritis accounting for an estimated 685 million cases and approximately 212,000 deaths globally per...

bcm.edu
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Congratulations to all the authors! 🎉
Soni Kaundal@sonik45620 Dec 2024
Our recent research from Prasad's lab reveals that human norovirus RdRp forms liquid-liquid phase condensates to drive replication in infected cells. #virology #phaseseparation @ScienceAdvances @EstesLab_BCM @anish12741503 @vijayalaks14983 @bcmhouston science.org/doi/10.1126/scia…

RNA-dependent RNA polymerase of predominant human norovirus forms liquid-liquid phase condensates...

Polymerase of a positive-sense RNA virus uses LLPS to regulate replication as an elegant solution for an enigmatic question.

science.org
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Check out our recent work in collaboration with @sakshipoddar20 and @kuruhoornambi
Cytoskeleton Journal@CytoskelJournal5 Sep 2024
Disruption of salt bridge interactions in the inter‐domain cleft of the tubulin‐like protein FtsZ of Escherichia coli makes cells sensitive to the cell division inhibitor PC190723 dlvr.it/TCrT0d
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The latest JBC cover shows an electron micrograph (background) of FtsZ filaments from Spiroplasma melliferum, a cell wall-less bacteria, and depicts that extended monomers and domain-swapped dimers are incompatible to form filaments. jbc.org/issue/S0021-9258(24)… #ASBMBJournals
On the Cover: FtsZ is a crucial cell division protein in bacteria, but it is unclear how it exhibits kinetic polarity during treadmilling. The cover shows an electron micrograph (background) of FtsZ filaments from Spiroplasma melliferum, a cell wall-less bacteria. Additionally, the illustration depicts that extended monomers and domain-swapped dimers are incompatible to form filaments, and that monomer addition occurs from the bottom of the filament (center), representing the kinetic polarity of FtsZ filaments.

ALT On the Cover: FtsZ is a crucial cell division protein in bacteria, but it is unclear how it exhibits kinetic polarity during treadmilling. The cover shows an electron micrograph (background) of FtsZ filaments from Spiroplasma melliferum, a cell wall-less bacteria. Additionally, the illustration depicts that extended monomers and domain-swapped dimers are incompatible to form filaments, and that monomer addition occurs from the bottom of the filament (center), representing the kinetic polarity of FtsZ filaments.

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Excited to share our latest research featured on the cover of @jbiolchem ! June 2024, Volume 300, Number 6.
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The cover shows an electron micrograph (background) of FtsZ filaments from Spiroplasma melliferum, a cell wall-less bacteria.
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Additionally, the illustration depicts that extended monomers and domain-swapped dimers are incompatible to form filaments, and that monomer addition occurs from the bottom of the filament (center), representing the kinetic polarity of FtsZ filaments.
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New in JBC press: "Dynamics of interdomain rotation facilitates FtsZ filament assembly." Learn more: jbc.org/article/S0021-9258(2…
Figure 2. SmFtsZ polymerizes to form rings in E. coli in vivo.

ALT Figure 2. SmFtsZ polymerizes to form rings in E. coli in vivo.

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Thanks to all the authors- @soumyashuvro @VaishnaviPB @ShrikantHarne1 and Dr Gayathri. Thanks to @kuruhoornambi and @sakshipoddar20 for the great collaboration!
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So excited to hear not one but TWO fantastic #WomenInSTEM talk about their ground-breaking research at our 49th Annual McLean Lectures! @SteitzLab @LugerLab @bcmhouston #RNA #NucleicAcids #Histones because you know it's ALL ABOUT THAT BASE! (see: youtu.be/gwy2lD1reos?si=Y6OR…).
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IISER Pune@IISERPune9 Sep 2023
Dr. Gayathri Pananghat from #IISERPune is among recent awardees for S. Ramachandran National Bioscience Award from @DBTIndia!! Dr. Pananghat's research is on understanding the molecular basis of cell shape and motility Our #Congrats and best wishes!! iiserpune.ac.in/news/post/db…
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Nature Microbiology@NatureMicrobiol2 May 2023
📣OUT NOW Bacterial cell division afficionados take note! Incredible depth of detail using cryo-EM 🔬to delineate the structure of the bacterial divisome core complex, and antibiotic target, FtsWIQBL. At 3.7 Å resolution. nature.com/articles/s41564-0…

Cryo-EM structure of the bacterial divisome core complex and antibiotic target FtsWIQBL

Nature Microbiology - The cryogenic electron microscopy structure of the Pseudomonas aeruginosa cell division complex and antibiotic drug target, FtsWIQBL, suggests a possible activation mechanism.

nature.com
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Matthew Clark@Matthew_BaTiSiO2 Feb 2023
This incredible structure is the Light Harvesting Complex of photosynthetic red algae It acts like a satellite dish to capture photons and channel them into the Photosystem reaction center PDB 7Y5E with the help of @bradyajohnston's Molecular nodes #Animation #Blender #Science
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