T
Thomas E. Ellenberger
Researcher at Harvard University
Publications - 13
Citations - 2383
Thomas E. Ellenberger is an academic researcher from Harvard University. The author has contributed to research in topics: DNA & Leucine zipper. The author has an hindex of 10, co-authored 13 publications receiving 2315 citations.
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Journal ArticleDOI
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α Helices: Crystal structure of the protein-DNA complex
TL;DR: The details of the bZIP dimer interaction with DNA can explain recognition of the AP-1 site by the GCN4 protein.
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DNA helicase Srs2 disrupts the Rad51 presynaptic filament
Lumir Krejci,Stephen Van Komen,Ying Li,Jana Villemain,Mothe Sreedhar Reddy,Hannah L. Klein,Thomas E. Ellenberger,Patrick Sung +7 more
TL;DR: The role of SRS2 in recombination modulation is clarified by purifying its encoded product and examining its interactions with the Rad51 recombinase, and it is shown that Srs2 acts by dislodging Rad51 from ssDNA.
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Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA.
Michael A. Weiss,Thomas E. Ellenberger,C R Wobbe,Jeng-Shin Lee,Stephen C. Harrison,Kevin Struhl +5 more
TL;DR: The results indicate that the GCN4 basic region is significantly unfolded at 25 °C and that its folded, α-helical conformation is stabilized by binding to DNA.
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Primary structure of the gene encoding the bifunctional dihydrofolate reductase-thymidylate synthase of Leishmania major.
TL;DR: Comparisons of the DHFR-TS sequence with DHFR and TS sequences of other organisms indicate that the order of enzymatic activities within the bifunctional polypeptide chain is DHFR followed by TS, and the Leishmania bifunctionsal DH FR-TS evolved independently and not through a phage T4-related intermediate.
Journal ArticleDOI
Role of ATP Hydrolysis in the Antirecombinase Function of Saccharomyces cerevisiae Srs2 Protein
Lumir Krejci,Margaret A. Macris,Ying Li,Stephen Van Komen,Jana Villemain,Thomas E. Ellenberger,Hannah L. Klein,Patrick Sung +7 more
TL;DR: Two mutant variants that are altered in the Walker type A sequence involved in the binding and hydrolysis of ATP are constructed that highlight the importance of the ATP hydrolysisfueled DNA motor activity in SRS2 functions.