A collection of chimeric pore-forming domains between colicins A and B was constructed to investigate the specific determinants responsible for recognition by the corresponding immunity proteins. The fusion sites in the hybrid proteins were positioned according to the three-dimensional structure of the soluble form of the colicin A pore-forming domain. The hydrophobic hairpin of colicin pore-forming domains, buried in the core of the soluble structure, was the main determinant recognized by the integral immunity proteins. The immunity protein function may require helix-helix recognition within the lipid bilayer.
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http://dx.doi.org/10.1128/jb.174.20.6432-6437.1992 | DOI Listing |
Nat Commun
January 2025
Department of Pharmacology, Yale University School of Medicine, New Haven, CT, 06520, USA.
Sevenless, the Drosophila homologue of ROS1 (University of Rochester Sarcoma) (herein, dROS1) is a receptor tyrosine kinase (RTK) essential for the differentiation of Drosophila R7 photoreceptor cells. Activation of dROS1 is mediated by binding to the extracellular region (ECR) of the GPCR (G protein coupled receptor) BOSS (Bride Of Sevenless) on adjacent cells. Activation of dROS1 by BOSS leads to subsequent downstream signaling pathways including SOS (Son of Sevenless).
View Article and Find Full Text PDFInt J Mol Sci
December 2024
Institute of Food Technology, Department of Food Science and Technology, BOKU University, 1190 Vienna, Austria.
is a potential bacterial cell factory to develop delivery systems for vaccines and therapeutic proteins. Much progress has been made in applications using engineered against, e.g.
View Article and Find Full Text PDFBiochim Biophys Acta Biomembr
January 2025
Biochemistry and Molecular Biology Department, Center for Pharmaceutical Research and Development, Ave. 26 # 1605, Nuevo Vedado, Ciudad de La Habana, 10400, Cuba. Electronic address:
Acylation is a common method used to modify antimicrobial peptides to enhance their effectiveness. It increases the interactions between the peptide and the bacterial cell membranes. However, acylation can also reduce the selectivity of the peptides by making them more active on eukaryotic membranes, which can lead to unintended toxicity.
View Article and Find Full Text PDFRSC Adv
November 2024
Institute of Physics, Faculty of Mathematics and Physics, Charles University Ke Karlovu 5, 121 16 Prague 2 Czech Republic +420 95155 1471.
Recently published observations have highlighted the presence of cruciform structures within the genome, suggesting their potential significance in the rapid recognition of the target sequence for transcription factor binding. In this study, we investigate the organization and stability of the (coding) strand within the Serum Response Element of the gene promoter ( SRE), specifically focusing on segments spanning 12 to 36 nucleotides, centered around the CArG-box. Through a thorough examination of UV absorption patterns with varying temperatures, we identified the emergence of a remarkably stable structure, which we conclusively characterized as a hairpin using complementary H NMR experiments.
View Article and Find Full Text PDFBiosens Bioelectron
March 2025
Key Laboratory of Laboratory Medicine, Ministry of Education, Zhejiang Provincial Key Laboratory of Medical Genetics, Cixi Biomedical Research Institute, School of Laboratory Medicine and Life sciences, Wenzhou Medical University, Wenzhou, 325035, China. Electronic address:
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