ArticleThe Journal of biological chemistry2015
Apoglobin Stability Is the Major Factor Governing both Cell-free and in Vivo Expression of Holomyoglobin.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- Resurrecting lost ancient myoglobin proteins to elucidate mechanisms of diving adaptation in mammals.Biophysics and physicobiology · 2026Article
- Digital Microfluidics-Driven Cell-Free Protein Synthesis Platform Reveals Expression and Stability Determinants for Phytoglobins and Cysteine-to-Alanine Substituted Variants.Antioxidants (Basel, Switzerland) · 2025Article
- Deep mutational scanning reveals a de novo disulfide bond and combinatorial mutations for engineering thermostable myoglobin.Protein science : a publication of the Protein Society · 2025Article
- Precise Engineering and Efficient Biosynthesis of Robust and High-Activity Human Haemoglobin for Artificial Oxygen Carriers.Microbial biotechnology · 2025Article
- In silico protein dynamics in the human cytoplasm: Partial folding, misfolding, fold switching, and non-native interactions.Protein science : a publication of the Protein Society · 2023Article
- Structural and oxidative investigation of a recombinant high-yielding fetal hemoglobin mutant.Frontiers in molecular biosciences · 2023Article
- Kinetic mechanisms for OMolecular aspects of medicine · 2022Review
- Common and unique strategies of myoglobin evolution for deep-sea adaptation of diving mammals.iScience · 2021Article
- Article
- Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology.Frontiers in molecular biosciences · 2021Review
- Introducing Negatively Charged Residues on the Surface of Fetal Hemoglobin Improves Yields inFrontiers in bioengineering and biotechnology · 2021Article
- Atomistic Simulations of Heme Dissociation Pathways in Human Methemoglobins Reveal Hidden Intermediates.Biochemistry · 2020Article
- The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.Biophysical journal · 2020Article
- Lessons Learned from 50 Years of Hemoglobin Research: Unstirred and Cell-Free Layers, Electrostatics, Baseball Gloves, and Molten Globules.Antioxidants & redox signaling · 2020Review
- Current Challenges in the Development of Acellular Hemoglobin Oxygen Carriers by Protein Engineering.Shock (Augusta, Ga.) · 2019Review
- Myoglobin maturation is driven by the hsp90 chaperone machinery and by soluble guanylyl cyclase.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Emergence of a Chimeric Globin Pseudogene and Increased Hemoglobin Oxygen Affinity Underlie the Evolution of Aquatic Specializations in Sirenia.Molecular biology and evolution · 2019Article
- Tracing whale myoglobin evolution by resurrecting ancient proteins.Scientific reports · 2018Article
- Replacement of the Distal Histidine Reveals a Noncanonical Heme Binding Site in a 2-on-2 Hemoglobin.Biochemistry · 2018Article
- Ecobody technology: rapid monoclonal antibody screening method from single B cells using cell-free protein synthesis for antigen-binding fragment formation.Scientific reports · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Expression levels in animal muscle tissues and in Escherichia coli vary widely for naturally occurring mammalian myoglobins (Mb). To explore this variation, we developed an in vitro transcription and wheat germ extract-based translation assay to examine quantitatively the factors that govern expression of holoMb. We constructed a library of naturally occurring Mbs from two terrestrial and four deep-diving aquatic mammals and three distal histidine mutants designed to enhance apoglobin stability but decrease hemin affinity. A strong linear correlation is observed between cell-free expression levels of holo-metMb variants and their corresponding apoglobin stabilities, which were measured independently by guanidine HCl-induced unfolding titrations using purified proteins. In contrast, there is little dependence of expression on hemin affinity. Our results confirm quantitatively that deep diving mammals have highly stable Mbs that express to higher levels in animal myocytes, E. coli, and the wheat germ cell-free system than Mbs from terrestrial mammals. Our theoretical analyses show that the rate of aggregation of unfolded apoMb is very large, and as a result, the key factor for high level expression of holoMb, and presumably other heme proteins, is an ultra high fraction of folded, native apoglobin that is capable of rapidly binding hemin. This fraction is determined by the overall equilibrium folding constant and not hemin affinity. These results also demonstrate that the cell-free transcription/translation system can be used as a high throughput platform to screen for apoglobin stability without the need to generate large amounts of protein for in vitro unfolding measurements.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.