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lizzthrall.bsky.social

@lizzthrall.bsky.social
11 followers 32 following 4 posts
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lizzthrall.bsky.social @lizzthrall.bsky.social · 05/08/2025
These results give new insight into the B. subtilis replisome and also raise some interesting new questions. Thanks to all the students who made this possible, and to Xindan Wang and Nick Sawyer for a great collaboration between our labs! (4/4)
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lizzthrall.bsky.social @lizzthrall.bsky.social · 05/08/2025
Combining biochemistry, microbiological assays, and in vivo single-molecule fluorescence imaging, we show that the PolC-DnaN interaction is essential. But surprisingly, although DnaE binds DnaN weakly, that interaction is entirely dispensable for replication. (3/4)
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lizzthrall.bsky.social @lizzthrall.bsky.social · 05/08/2025
Unlike the model species E. coli, B. subtilis has two essential replicative pols, PolC and DnaE. They must exchange frequently in replication, but it’s not clear how their activity is coordinated. We investigated the role of PolC and DnaE interactions with the clamp in replication. (2/4)
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lizzthrall.bsky.social @lizzthrall.bsky.social · 05/08/2025
Excited to share another study from my lab @fordhamchem now out @narjournal.bsky.social‬: doi.org/10.1093/nar/.... Most bacterial DNA polymerases must interact with the sliding clamp DnaN for their function, but we show that it’s more complicated in B. subtilis DNA replication. (1/4)
doi.org
The B. subtilis replicative polymerases bind the sliding clamp with different strengths to tune their activity in DNA replication
Abstract. Ring-shaped sliding clamp proteins are essential components of the replication machinery across all domains of life. DNA polymerases bind the cla
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