Linked Life Data

18163650

Source:http://linkedlifedata.com/resource/pubmed/id/18163650

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-1-15
pubmed:abstractText
Phototropin (phot) is a blue-light sensor protein that elicits several photo responses in plants. Phototropin has two flavin mononucleotide (FMN)-binding domains, LOV1 and LOV2, in its N-terminal half. The C-terminal half is a blue-light-regulated Ser/Thr kinase. Various functional studies have reported that only LOV2 is responsible for the kinase activity, whereas the X-ray crystallographic structures of the LOV1 and LOV2 domains are almost identical. How does such a functional difference emerge? Our previous FTIR study of the LOV domains of Adiantum neochrome1 (neo1) showed that light-induced protein structural changes are small and temperature independent for neo1-LOV1, whereas the structural changes are large and highly temperature dependent for neo1-LOV2, which involve loops, alpha-helices, and beta-sheets. These observations successfully explained the different functions in terms of protein structural changes. They also suggested the presence of some crucial amino acids responsible for greater protein structural changes in the LOV2 domain. Here, we focused on phenylalanine-1010 (Phe1010) in neo1-LOV2, where FMN is sandwiched between Phe1010 and the reactive cysteine. Phenylalanine at this position is conserved for LOV2 domains, while the corresponding amino acid is leucine for LOV1 domains in almost all plant phototropins. We observed that unlike wild-type LOV2, the FTIR spectra of F1010L LOV2 exhibited no temperature dependence in the alpha-helical and beta-sheet regions and that spectral changes in amide-I of these regions were significantly reduced, which was similar to LOV1. Thus, the replacement of phenylalanine with leucine converts neo1-LOV2 into neo1-LOV1 in terms of protein structural changes that must be related to the different functions. We will discuss the roles of phenylalanine and leucine in the LOV2 and LOV1 domains, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
922-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18163650-Adiantum, pubmed-meshheading:18163650-Amino Acid Substitution, pubmed-meshheading:18163650-Cryptochromes, pubmed-meshheading:18163650-Darkness, pubmed-meshheading:18163650-Flavin Mononucleotide, pubmed-meshheading:18163650-Flavoproteins, pubmed-meshheading:18163650-Kinetics, pubmed-meshheading:18163650-Light, pubmed-meshheading:18163650-Models, Molecular, pubmed-meshheading:18163650-Phenylalanine, pubmed-meshheading:18163650-Photochemistry, pubmed-meshheading:18163650-Plant Proteins, pubmed-meshheading:18163650-Protein Structure, Secondary, pubmed-meshheading:18163650-Protein Structure, Tertiary, pubmed-meshheading:18163650-Recombinant Proteins, pubmed-meshheading:18163650-Spectrophotometry, pubmed-meshheading:18163650-Spectrophotometry, Ultraviolet, pubmed-meshheading:18163650-Spectroscopy, Fourier Transform Infrared, pubmed-meshheading:18163650-Temperature
pubmed:year
2008
pubmed:articleTitle
Role of Phe1010 in light-induced structural changes of the neo1-LOV2 domain of Adiantum.
pubmed:affiliation
Department of Materials Science and Engineering, Nagoya Institute of Technology, Showa-ku, Nagoya 466-8555, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't