Keren Lasker
@kerenlasker.bsky.social
Membraneless Organelles in Bacteria: Structure, Dynamics, Function, and Engineering. Assistant Professor @scripps.edu.
https://laskerlab.org/
https://laskerlab.org/
Part 2 is starting soon! 🤩
February 15, 2025 at 6:22 PM
Part 2 is starting soon! 🤩
Part I of BIV subgroup starts in an hour (8:30 am PT)
Join us!
Join us!
February 15, 2025 at 3:39 PM
Part I of BIV subgroup starts in an hour (8:30 am PT)
Join us!
Join us!
🚀 Join us at #BPS2025 tomorrow at 8:30 AM for a spectacular lineup of cutting-edge methods & biology in Biopolymers In Vivo! 🧪🔬
🧠 AI & IDP phase behavior | 🌱 Protein thermosensing | ❄️ Cryo-EM
🧬 GTPase activity | 🛠️ Engineered condensates | 🤖 Deep learning | 💧 Phase separation
🧠 AI & IDP phase behavior | 🌱 Protein thermosensing | ❄️ Cryo-EM
🧬 GTPase activity | 🛠️ Engineered condensates | 🤖 Deep learning | 💧 Phase separation
February 15, 2025 at 12:05 AM
🚀 Join us at #BPS2025 tomorrow at 8:30 AM for a spectacular lineup of cutting-edge methods & biology in Biopolymers In Vivo! 🧪🔬
🧠 AI & IDP phase behavior | 🌱 Protein thermosensing | ❄️ Cryo-EM
🧬 GTPase activity | 🛠️ Engineered condensates | 🤖 Deep learning | 💧 Phase separation
🧠 AI & IDP phase behavior | 🌱 Protein thermosensing | ❄️ Cryo-EM
🧬 GTPase activity | 🛠️ Engineered condensates | 🤖 Deep learning | 💧 Phase separation
14b/ In filament-deficient mutants, DNA segregation and cell division are disrupted. Without filaments, PopZ fails to anchor ParB effectively, leading to cellular dysfunction.
December 30, 2024 at 9:01 PM
14b/ In filament-deficient mutants, DNA segregation and cell division are disrupted. Without filaments, PopZ fails to anchor ParB effectively, leading to cellular dysfunction.
14a/ Why does this matter? 🧬
Replacing PopZ with a filament-deficient mutant is toxic to Caulobacter crescentus. To investigate, we tagged ParB, a protein anchored by PopZ and crucial for DNA segregation. 🔍✨
December 30, 2024 at 9:01 PM
14a/ Why does this matter? 🧬
Replacing PopZ with a filament-deficient mutant is toxic to Caulobacter crescentus. To investigate, we tagged ParB, a protein anchored by PopZ and crucial for DNA segregation. 🔍✨
12/ Multiscale assembly of PopZ condensation
Putting it all together ⬇️
Putting it all together ⬇️
December 30, 2024 at 9:01 PM
12/ Multiscale assembly of PopZ condensation
Putting it all together ⬇️
Putting it all together ⬇️
11/ Two jobs, one switch!
In the dilute phase, the client-binding region binds the OD region needed for assembly.
Upon condensation, an IDR-driven conformational change:
1️⃣ Reveals OD interfaces for condensate formation.
2️⃣ Exposes client-binding sites to recruit partners.
A molecular multitasker!
In the dilute phase, the client-binding region binds the OD region needed for assembly.
Upon condensation, an IDR-driven conformational change:
1️⃣ Reveals OD interfaces for condensate formation.
2️⃣ Exposes client-binding sites to recruit partners.
A molecular multitasker!
December 30, 2024 at 9:01 PM
11/ Two jobs, one switch!
In the dilute phase, the client-binding region binds the OD region needed for assembly.
Upon condensation, an IDR-driven conformational change:
1️⃣ Reveals OD interfaces for condensate formation.
2️⃣ Exposes client-binding sites to recruit partners.
A molecular multitasker!
In the dilute phase, the client-binding region binds the OD region needed for assembly.
Upon condensation, an IDR-driven conformational change:
1️⃣ Reveals OD interfaces for condensate formation.
2️⃣ Exposes client-binding sites to recruit partners.
A molecular multitasker!
9/ The OD drives condensation, while the IDR inhibits it:
By separating the OD from the IDR, we uncovered:
1️⃣ The OD is necessary and sufficient for condensation.
2️⃣ OD-only condensates are filamentous, resembling those formed by the full-length protein.
3️⃣ The IDR inhibits condensation
By separating the OD from the IDR, we uncovered:
1️⃣ The OD is necessary and sufficient for condensation.
2️⃣ OD-only condensates are filamentous, resembling those formed by the full-length protein.
3️⃣ The IDR inhibits condensation
December 30, 2024 at 9:01 PM
9/ The OD drives condensation, while the IDR inhibits it:
By separating the OD from the IDR, we uncovered:
1️⃣ The OD is necessary and sufficient for condensation.
2️⃣ OD-only condensates are filamentous, resembling those formed by the full-length protein.
3️⃣ The IDR inhibits condensation
By separating the OD from the IDR, we uncovered:
1️⃣ The OD is necessary and sufficient for condensation.
2️⃣ OD-only condensates are filamentous, resembling those formed by the full-length protein.
3️⃣ The IDR inhibits condensation
7b/ The Isodesmic Model:
PopZ filaments assemble via a non-cooperative isodesmic model—binding affinities stay constant regardless of filament length.
PopZ filaments assemble via a non-cooperative isodesmic model—binding affinities stay constant regardless of filament length.
December 30, 2024 at 9:01 PM
7b/ The Isodesmic Model:
PopZ filaments assemble via a non-cooperative isodesmic model—binding affinities stay constant regardless of filament length.
PopZ filaments assemble via a non-cooperative isodesmic model—binding affinities stay constant regardless of filament length.
7a/ PopZ condensates are filamentous
Using cryo-ET (in collaboration with the Park Lab), we revealed that PopZ condensates are built from filaments—a crucial insight into their structural organization.
Using cryo-ET (in collaboration with the Park Lab), we revealed that PopZ condensates are built from filaments—a crucial insight into their structural organization.
December 30, 2024 at 9:01 PM
7a/ PopZ condensates are filamentous
Using cryo-ET (in collaboration with the Park Lab), we revealed that PopZ condensates are built from filaments—a crucial insight into their structural organization.
Using cryo-ET (in collaboration with the Park Lab), we revealed that PopZ condensates are built from filaments—a crucial insight into their structural organization.
6/ The building blocks of PopZ:
PopZ is modular, featuring three key regions:
• A C-terminal oligomerization domain (OD) that drives condensation
• A negatively charged, proline-rich IDR that regulates fluidity
• An N-terminal helical region (H1) that binds clients
PopZ is modular, featuring three key regions:
• A C-terminal oligomerization domain (OD) that drives condensation
• A negatively charged, proline-rich IDR that regulates fluidity
• An N-terminal helical region (H1) that binds clients
December 30, 2024 at 9:01 PM
6/ The building blocks of PopZ:
PopZ is modular, featuring three key regions:
• A C-terminal oligomerization domain (OD) that drives condensation
• A negatively charged, proline-rich IDR that regulates fluidity
• An N-terminal helical region (H1) that binds clients
PopZ is modular, featuring three key regions:
• A C-terminal oligomerization domain (OD) that drives condensation
• A negatively charged, proline-rich IDR that regulates fluidity
• An N-terminal helical region (H1) that binds clients
5/ Meet PopZ:
PopZ is a small, largely disordered protein that helps microbes 🦠 in α-proteobacteria organize their cytoplasm.
We study C. crescentus PopZ, discovered in 2008.
Check out this tomogram (previous work with @thevillalab.bsky.social) showing PopZ forming ribosome-free microdomains!
PopZ is a small, largely disordered protein that helps microbes 🦠 in α-proteobacteria organize their cytoplasm.
We study C. crescentus PopZ, discovered in 2008.
Check out this tomogram (previous work with @thevillalab.bsky.social) showing PopZ forming ribosome-free microdomains!
December 30, 2024 at 9:01 PM
5/ Meet PopZ:
PopZ is a small, largely disordered protein that helps microbes 🦠 in α-proteobacteria organize their cytoplasm.
We study C. crescentus PopZ, discovered in 2008.
Check out this tomogram (previous work with @thevillalab.bsky.social) showing PopZ forming ribosome-free microdomains!
PopZ is a small, largely disordered protein that helps microbes 🦠 in α-proteobacteria organize their cytoplasm.
We study C. crescentus PopZ, discovered in 2008.
Check out this tomogram (previous work with @thevillalab.bsky.social) showing PopZ forming ribosome-free microdomains!