@article{BrechunArndtWoolley2017,
  author    = {Brechun, Katherine E. and Arndt, Katja Maren and Woolley, G. Andrew},
  title     = {Strategies for the photo-control of endogenous protein activity},
  series = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  volume    = {45},
  journal   = {Current opinion in structural biology : review of all advances ; evaluation of key references ; comprehensive listing of papers},
  publisher = {Elsevier},
  address   = {London},
  issn      = {0959-440X},
  doi       = {10.1016/j.sbi.2016.11.014},
  pages     = {53 -- 58},
  year      = {2017},
  language  = {en}
}
@phdthesis{Brechun2019,
  author    = {Brechun, Katherine E.},
  title     = {Development and application of genetic networks for engineering photo-controlled proteins},
  doi       = {10.25932/publishup-43092},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-430924},
  school      = {Universit{\"a}t Potsdam},
  pages     = {xxiv, 195},
  year      = {2019},
  abstract  = {Light-switchable proteins are being used increasingly to understand and manipulate complex molecular systems. The success of this approach has fueled the development of tailored photo-switchable proteins, to enable targeted molecular events to be studied using light. The development of novel photo-switchable tools has to date largely relied on rational design. Complementing this approach with directed evolution would be expected to facilitate these efforts. Directed evolution, however, has been relatively infrequently used to develop photo-switchable proteins due to the challenge presented by high-throughput evaluation of switchable protein activity. This thesis describes the development of two genetic circuits that can be used to evaluate libraries of switchable proteins, enabling optimization of both the on- and off-states. A screening system is described, which permits detection of DNA-binding activity based on conditional expression of a fluorescent protein. In addition, a tunable selection system is presented, which allows for the targeted selection of protein-protein interactions of a desired affinity range. This thesis additionally describes the development and characterization of a synthetic protein that was designed to investigate chromophore reconstitution in photoactive yellow protein (PYP), a promising scaffold for engineering photo-controlled protein tools.},
  language  = {en}
}
@article{BrechunZhenJaikaranetal.2019,
  author    = {Brechun, Katherine E. and Zhen, Danlin and Jaikaran, Anna and Borisenko, Vitali and Kumauchi, Masato and Hoff, Wouter D. and Arndt, Katja Maren and Woolley, Andrew G},
  title     = {Detection of Incorporation of p-Coumaric Acid into Photoactive Yellow Protein Variants in Vivo},
  series = {Biochemistry},
  volume    = {58},
  journal   = {Biochemistry},
  number    = {23},
  publisher = {American Chemical Society},
  address   = {Washington},
  issn      = {0006-2960},
  doi       = {10.1021/acs.biochem.9b00279},
  pages     = {2682 -- 2694},
  year      = {2019},
  abstract  = {We report the design and characterization of photoactive yellow protein (PYP)-blue fluorescent protein (mTagBFP) fusion constructs that permit the direct assay of reconstitution and function of the PYP domain. These constructs allow for in vivo testing of co-expression systems for enzymatic production of the p-coumaric acid-based PYP chromophore, via the action of tyrosine ammonia lyase and p-coumaroyl-CoA ligase (pCL or 4CL). We find that different 4CL enzymes can function to reconstitute PYP, including 4CL from Arabidopsis thaliana that can produce similar to 100\% holo-PYP protein under optimal conditions. mTagBFP fusion constructs additionally enable rapid analysis of effects of mutations on PYP photocycles. We use this mTagBFP fusion strategy to demonstrate in vivo reconstitution of several PYP-based optogenetic tools in Escherichia coli via a biosynthesized chromophore, an important step for the use of these optogenetic tools in vivo in diverse hosts.},
  language  = {en}
}
@article{MazumderBrechunKimetal.2015,
  author    = {Mazumder, Mostafizur and Brechun, Katherine E. and Kim, Yongjoo B. and Hoffmann, Stefan A. and Chen, Yih Yang and Keiski, Carrie-Lynn and Arndt, Katja Maren and McMillen, David R. and Woolley, G. Andrew},
  title     = {An Escherichia coli system for evolving improved light-controlled DNA-binding proteins},
  series = {Protein engineering design \& selection},
  volume    = {28},
  journal   = {Protein engineering design \& selection},
  number    = {9},
  publisher = {Oxford Univ. Press},
  address   = {Oxford},
  issn      = {1741-0126},
  doi       = {10.1093/protein/gzv033},
  pages     = {293 -- 302},
  year      = {2015},
  abstract  = {Light-switchable proteins offer numerous opportunities as tools for manipulating biological systems with exceptional degrees of spatiotemporal control. Most designed light-switchable proteins currently in use have not been optimised using the randomisation and selection/screening approaches that are widely used in other areas of protein engineering. Here we report an approach for screening light-switchable DNA-binding proteins that relies on light-dependent repression of the transcription of a fluorescent reporter. We demonstrate that the method can be used to recover a known light-switchable DNA-binding protein from a random library.},
  language  = {en}
}
@misc{BrechunWoolleyArndt2017,
  author    = {Brechun, Katherine E. and Woolley, Andrew and Arndt, Katja Maren},
  title     = {A Bacterial Bandpass Assay for Protein-Protein Interactions},
  series = {Protein science : a publication of the Protein Society},
  volume    = {26},
  journal   = {Protein science : a publication of the Protein Society},
  publisher = {Wiley},
  address   = {Hoboken},
  issn      = {0961-8368},
  pages     = {198 -- 198},
  year      = {2017},
  language  = {en}
}