Single Amino Acid Replacement Makes Aequorea victoria Fluorescent Proteins Reversibly Photoswitchable (Articolo in rivista)

Type
Label
  • Single Amino Acid Replacement Makes Aequorea victoria Fluorescent Proteins Reversibly Photoswitchable (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/ja9014953 (literal)
Alternative label
  • Bizzarri R., Serresi M., Cardarelli F., Abbruzzetti S., Campanini B., Viappiani C., Beltram F. (2010)
    Single Amino Acid Replacement Makes Aequorea victoria Fluorescent Proteins Reversibly Photoswitchable
    in Journal of the American Chemical Society (Print)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bizzarri R., Serresi M., Cardarelli F., Abbruzzetti S., Campanini B., Viappiani C., Beltram F. (literal)
Pagina inizio
  • 85 (literal)
Pagina fine
  • 95 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 132 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 11 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1. IIT NEST, Ctr Nanotechnol Innovat, I-56127 Pisa, Italy 2. Scuola Normale Super Pisa, NEST, I-56127 Pisa, Italy 3. CNR, INFM, I-56127 Pisa, Italy 4. Univ Parma, Dipartimento Fis, I-43100 Parma, Italy 5. Univ Parma, Dipartimento Biochim & Biol Mol, I-43100 Parma, Italy (literal)
Titolo
  • Single Amino Acid Replacement Makes Aequorea victoria Fluorescent Proteins Reversibly Photoswitchable (literal)
Abstract
  • Reversibly photoswitchable (i.e., photochromic) fluorescent proteins open the way to a number of advanced bioimaging techniques applicable to living-cell studies such as sequential photolabeling of distinct cellular regions, innovative FRET schemes, or nanoscopy. Owing to the relevance of fluorescent proteins from Aequorea victoria (AFPs) for cell biology, a photochromic \"toolbox\" constituted by several AFPs is highly desirable. Here we introduce four new photochromic AFPs whose reversible photoswitching occurs between the native bright and a dark state at low illumination power, on account of a very efficient cis-trans photoisomerization. Most remarkably, the optical bistability of these AFPs derives from the single E222Q mutation in the primary sequence. Apparently, the E222Q substitution can restore the intrinsic photochromic behavior of the isolated chromophore. The significance of these mutants for high-resolution in vivo cell imaging is shown by means of photochromic FRET experiments. (literal)
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