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Full-Text Articles in Biomedical Engineering and Bioengineering

Blue-Light Induced Biosynthesis Of Ros Contributes To The Signaling Mechanism Of Arabidopsis Cryptochrome, Mohamed A. El-Esawi, Louis David Arthaut, Nathalie Jourdan, Alain D'Harlingue, Justin J. Link, Margaret Ahmad, Carlos F. Martino Dec 2017

Blue-Light Induced Biosynthesis Of Ros Contributes To The Signaling Mechanism Of Arabidopsis Cryptochrome, Mohamed A. El-Esawi, Louis David Arthaut, Nathalie Jourdan, Alain D'Harlingue, Justin J. Link, Margaret Ahmad, Carlos F. Martino

Biomedical Engineering and Sciences Faculty Publications

Cryptochromes are evolutionarily conserved blue light receptors with many roles throughout plant growth and development. They undergo conformational changes in response to light enabling interaction with multiple downstream signaling partners. Recently, it has been shown that cryptochromes also synthesize reactive oxygen species (ROS) in response to light, suggesting the possibility of an alternate signaling mechanism. Here we show by fluorescence imaging and microscopy that H202 and ROS accumulate in the plant nucleus after cryptochrome activation. They induce ROS-regulated transcripts including for genes implicated in pathogen defense, biotic and abiotic stress. Mutant cryptochrome alleles that are non-functional in photomorphogenesis retain the …


Decoding And Reprogramming Fungal Iterative Nonribosomal Peptide Synthetases, Daya Yu, Fuchao Xu, Shuwei Zhang, Jixun Zhan May 2017

Decoding And Reprogramming Fungal Iterative Nonribosomal Peptide Synthetases, Daya Yu, Fuchao Xu, Shuwei Zhang, Jixun Zhan

Biological Engineering Faculty Publications

Nonribosomal peptide synthetases (NRPSs) assemble a large group of structurally and functionally diverse natural products. While the iterative catalytic mechanism of bacterial NRPSs is known, it remains unclear how fungal NRPSs create products of desired length. Here we show that fungal iterative NRPSs adopt an alternate incorporation strategy. Beauvericin and bassianolide synthetases have the same C1-A1-T1-C2-A2-MT-T2a-T2b-C3 domain organization. During catalysis, C3 and C2 take turns to incorporate the two biosynthetic precursors into the growing depsipeptide chain that swings between T1 and T …