Zn2+-Mediated Structure Formation and Compaction of the “Natively Unfolded” Human Prothymosin α

Uversky, Vladimir N.; Gillespie, Joel R.; Millett, Ian S.; Khodyakova, Anna V.; Vasilenko, Raisa N.; Vasiliev, A. A.; Rodionov, I. L.; Kozlovskaya, Galina D.; Долгих, Д. А.; Fink, Anthony L.; Doniach, Sebastian; Permyakov, Eugene A.; Abramov, Vyacheslav M.

doi:10.1006/bbrc.1999.2013

Cited by 70 publications

(57 citation statements)

References 28 publications

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“…Again for structural purposes, there are numerous examples of divalent cation-binding stabilising folds of other IUPs, e.g. human sperm protamine and prothymosin-a by Zn 2þ (Gatewood et al, 1990;Uversky et al, 2000b). There are also exceptions, e.g.…”

Section: Mbp Binds Various Small Ligandsmentioning

confidence: 99%

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz

Ishiyama

Hill

et al. 2004

Micron

227

209

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Section: Mbp Binds Various Small Ligandsmentioning

confidence: 99%

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Harauz

Ishiyama

Hill

et al. 2004

Micron

227

209

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“…Rom et al (2006) also reported other zinc-binding phenomena relevance to ASR1-DNA interactions. The importance of zinc in mediating protein structure pertinent to its function has been further strengthened by studies on human prothymosin a, a protein characterized as natively unfolded (Uversky et al, 2000b) and also by zinc-driven folding and oligomerization of g-carbonic anhydrase (Simler et al, 2004). Folding of apo-metalloprotein has been reported to be induced by the binding of bivalent ions, including zinc (Ejnik et al, 2002), and the folding and stability of the nuclear hormone receptor DNAbinding domain was shown to be zinc dependent (Low et al, 2002).…”

Section: Zinc Binding and Desiccation Induce Order And Dimerization Imentioning

confidence: 99%

Desiccation and Zinc Binding Induce Transition of Tomato Abscisic Acid Stress Ripening 1, a Water Stress- and Salt Stress-Regulated Plant-Specific Protein, from Unfolded to Folded State

et al. 2006

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Abscisic acid stress ripening 1 (ASR1) is a low molecular weight plant-specific protein encoded by an abiotic stress-regulated gene. Overexpression of ASR1 in transgenic plants increases their salt tolerance. The ASR1 protein possesses a zinc-dependent DNA-binding activity. The DNA-binding site was mapped to the central part of the polypeptide using truncated forms of the protein. Two additional zinc-binding sites were shown to be localized at the amino terminus of the polypeptide. ASR1 protein is presumed to be an intrinsically unstructured protein using a number of prediction algorithms. The degree of order of ASR1 was determined experimentally using nontagged recombinant protein expressed in Escherichia coli and purified to homogeneity. Purified ASR1 was shown to be unfolded using dynamic light scattering, gel filtration, microcalorimetry, circular dichroism, and Fourier transform infrared spectrometry. The protein was shown to be monomeric by analytical ultracentrifugation. Addition of zinc ions resulted in a global change in ASR1 structure from monomer to homodimer. Upon binding of zinc ions, the protein becomes ordered as shown by Fourier transform infrared spectrometry and microcalorimetry, concomitant with dimerization. Tomato (Solanum lycopersicum) leaf soluble ASR1 is unstructured in the absence of added zinc and gains structure upon binding of the metal ion. The effect of zinc binding on ASR1 folding and dimerization is discussed.

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“…We have worked extensively with the 40 amino acid putative zinc binding region of prothymosin-␣, (ProT␣). This highly acidic, natively unfolded peptide has been shown to adopt an ordered structure upon zinc binding, but it does not contain any residues traditionally involved in zinc-binding such as cysteine, histidine, or methionine [22,23]. ProT␣ weakly binds as many as five zinc ions at pH 7 [24].…”

Section: Resultsmentioning

confidence: 99%

Zinc deposition during ESI-MS analysis of peptide-zinc complexes

Mattapalli

Monteith

Burns

et al. 2009

J. Am. Soc. Mass Spectrom.

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Electrospray ionization (ESI) mass spectrometry (MS) has proven to be an extremely powerful technique for studying the stoichiometry and binding strength of peptide-metal complexes. We have found a significant new problem in the ESI-MS of zinc-peptide systems involving the deposition of zinc in the ESI emitter. This deposition of zinc during the experiment removes a significant amount of zinc ions from the solution, impacting the resulting mass spectral intensities used to quantify the amount of the zinc-bound species. Analysis of infused zinc-peptide samples with atomic absorption spectrometry and with a custom-built nanoflow ESI source confirms the alteration of the analyte solutions with positive or negative or no potential applied to the emitter. Ultimately, the location of the zinc deposition was determined to be the stainless steel emitter. The use of a custom-built nanoESI interface using glass emitters was found to mitigate the zinc deposition problem. The phenomenon of metal deposition warrants further investigation as it may not be limited to just zinc and may represent a significant obstacle in the ESI-MS analysis of all protein-metal systems.

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Zn2+-Mediated Structure Formation and Compaction of the “Natively Unfolded” Human Prothymosin α

Cited by 70 publications

References 28 publications

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Myelin basic protein—diverse conformational states of an intrinsically unstructured protein and its roles in myelin assembly and multiple sclerosis

Desiccation and Zinc Binding Induce Transition of Tomato Abscisic Acid Stress Ripening 1, a Water Stress- and Salt Stress-Regulated Plant-Specific Protein, from Unfolded to Folded State

Zinc deposition during ESI-MS analysis of peptide-zinc complexes

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