Living cells must be able to respond to physiological and environmental fluctuations that threaten cell function and viability. A cellular event prone to disruption by a wide variety of internal and external perturbations is protein folding. To ensure protein folding can proceed under a range of conditions, the cell has evolved transcriptional, translational, and posttranslational signaling pathways to maintain folding homeostasis during cell stress. This review will focus on oxidative protein folding in the endoplasmic reticulum (ER) and will discuss the features of the main facilitator of biosynthetic disulfide bond formation, Ero1. Ero1 plays an essential role in setting the redox potential in the ER and regulation of Ero1 activity is central to maintain redox homeostasis and proper ER folding activity.
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http://dx.doi.org/10.1016/j.bbamcr.2007.12.011 | DOI Listing |
Protein Sci
February 2025
Department of Chemistry and Biochemistry, Center for RNA Biology, The Ohio State University, Columbus, Ohio, USA.
Loz1 is a zinc-responsive transcription factor in fission yeast that maintains cellular zinc homeostasis by repressing the expression of genes required for zinc uptake in high zinc conditions. Previous deletion analysis of Loz1 found a region containing two tandem CH zinc-fingers and an upstream "accessory domain" rich in histidine, lysine, and arginine residues to be sufficient for zinc-dependent DNA binding and gene repression. Here we report unexpected biophysical properties of this pair of seemingly classical CH zinc fingers.
View Article and Find Full Text PDFPest Manag Sci
January 2025
Department of Biological Sciences, University of Cincinnati, Cincinnati, OH, USA.
Background: Bed bugs are blood-feeders that rapidly proliferate into large indoor infestations. Their bites can cause allergies, secondary infections and psychological stress, among other problems. Although several tactics for their management have been used, bed bugs continue to spread worldwide wherever humans reside.
View Article and Find Full Text PDFBiotechnol Prog
January 2025
Graduate School of Interdisciplinary Science and Engineering in Health Systems, Okayama University, Okayama, Japan.
The production of disulfide-containing recombinant proteins often requires refolding of inclusion bodies before purification. A pre-refolding purification step is crucial for effective refolding because impurities in the inclusion bodies interfere with refolding and subsequent purification. This study presents a new pre-refolding procedure using a reversible S-cationization technique for protein solubilization and purification by reversed-phase high performance liquid chromatography.
View Article and Find Full Text PDFProtein Sci
February 2025
Amherst College, Amherst, Massachusetts, USA.
Hydrogen exchange mass spectrometry (HXMS) is a powerful tool to understand protein folding pathways and energetics. However, HXMS experiments to date have used exchange conditions termed EX1 or EX2 which limit the information that can be gained compared to the more general EXX exchange regime. If EXX behavior could be understood and analyzed, a single HXMS timecourse on an intact protein could fully map its folding landscape without requiring denaturation.
View Article and Find Full Text PDFEur J Med Chem
January 2025
Institute of Materia Medica, Chinese Academy of Medical Sciences, Peking Union Medical College, No. 1 Xian Nong Tan Street, Beijing, 100050, PR China; Key Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, 2019RU066, Lanzhou University, Lanzhou, 730000, PR China; Institute of Pharmaceutics, School of Pharmacy, 2019RU066, Lanzhou University, Lanzhou, 730000, PR China. Electronic address:
De novo design of antimicrobial peptides is a pivotal strategy for developing new antibacterial agents, leveraging its rapid and efficient nature. (XXYY), where X represents cationic residues, Y denotes hydrophobic residues, and n varies from 2 to 4, is a classical α-helix template. Based on which, numerous antimicrobial peptides have been synthesized.
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