ArticleProtein science : a publication of the Protein Society2000
Proline in alpha-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor.
Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Scaffold Hopping Transformations Using Auxiliary Restraints for Calculating Accurate Relative Binding Free Energies.Journal of chemical theory and computation · 2021Article
- Tolerance to Glutaraldehyde inFrontiers in microbiology · 2021Article
- Structural analysis of missense mutations occurring in the DNA-binding domain of HSF4 associated with congenital cataracts.Journal of structural biology: X · 2020Article
- Article
- The N-Terminal GYPSY Motif Is Required for Pilin-Specific Sortase SrtC1 Functionality in Lactobacillus rhamnosus Strain GG.PloS one · 2016Article
- Caspase-6 latent state stability relies on helical propensity.Biochemistry · 2011Article
- Critical biophysical properties in the Pseudomonas aeruginosa efflux gene regulator MexR are targeted by mutations conferring multidrug resistance.Protein science : a publication of the Protein Society · 2010Article
- Mapping essential domains of Mycobacterium smegmatis WhmD: insights into WhiB structure and function.Journal of bacteriology · 2006Article
- Inhibition of DNA binding by differential sumoylation of heat shock factors.Molecular and cellular biology · 2006Article
- Molecular markers of serine protease evolution.The EMBO journal · 2001Article
- The wing in yeast heat shock transcription factor (HSF) DNA-binding domain is required for full activity.Nucleic acids research · 2001Article
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2 authors at 1 institution in 1 country.
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Abstract
The DNA-binding domain of the yeast heat shock transcription factor (HSF) contains a strictly conserved proline that is at the center of a kink. To define the role of this conserved proline-centered kink, we replaced the proline with a number of other residues. These substitutions did not diminish the ability of the full-length protein to support growth of yeast or to activate transcription, suggesting that the proline at the center of the kink is not conserved for function. The stability of the isolated mutant DNA-binding domains was unaltered from the wild-type, so the proline is not conserved to maintain the stability of the protein. The crystal structures of two of the mutant DNA-binding domains revealed that the helices in the mutant proteins were still kinked after substitution of the proline, suggesting that the proline does not cause the alpha-helical kink. So why are prolines conserved in this and the majority of other kinked alpha-helices if not for structure, function, or stability? The mutant DNA-binding domains are less soluble than wild-type when overexpressed. In addition, the folding kinetics, as measured by stopped-flow fluorescence, is faster for the mutant proteins. These two results support the premise that the presence of the proline is critical for the folding pathway of HSF's DNA-binding domain. The finding may also be more general and explain why kinked helices maintain their prolines.
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