NDLI: Temperature-sensitive protein

Content Provider	PubMed Central
Author	Hauschild, Karl E. Metzler, Renee E. Arndt, Hans-dieter Moretti, Rocco Raffaelle, Marni Dervan, Peter B. Ansari, Aseem Z.
Copyright Year	2005
Abstract	Programmable DNA-binding polyamides coupled to short peptides have led to the creation of synthetic artificial transcription factors. A hairpin polyamide–YPWM tetrapeptide conjugate facilitates the binding of a natural transcription factor Exd to an adjacent DNA site. Such small molecules function as protein–DNA dimerizers that stabilize complexes at composite DNA binding sites. Here we investigate the role of the linker that connects the polyamide to the peptide. We find that a substantial degree of variability in the linker length is tolerated at lower temperatures. At physiological temperatures, the longest linker tested confers a “switch”-like property on the protein–DNA dimerizer, in that it abolishes the ability of the YPWM moiety to recruit the natural transcription factor to DNA. These observations provide design principles for future artificial transcription factors that can be externally regulated and can function in concert with the cellular regulatory circuitry.
Related Links	http://dx.doi.org/10.1073/pnas.0501289102
Ending Page	5013
Page Count	6
Starting Page	5008
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-04-05
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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