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Arabidopsis thaliana plastoglobule‐associated fibrillin 1a interacts with fibrillin 1b in vivo
Author(s) -
Gámez-Arjona Francisco Manuel,
de la Concepción Juan Carlos,
Raynaud Sandy,
Mérida Ángel
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.06.024
Subject(s) - fibrillin , thylakoid , microbiology and biotechnology , arabidopsis , plastid , biology , function (biology) , mechanism (biology) , chemistry , biochemistry , chloroplast , mutant , gene , extracellular matrix , philosophy , epistemology
Plant fibrillins are a well‐conserved protein family found in the plastids of all photosynthetic organisms, where they perform a wide range of functions. A number of these proteins have been suggested to be involved in the maintenance of thylakoids and the formation of plastoglobules, preventing their coalescence and favoring their clustering via an as‐yet unidentified cross‐linking mechanism. In this work we show that two members of this group, namely fibrillin 1a and 1b, interact with each other via a head‐to‐tail mechanism, thus raising the possibility that they form homo‐ or hetero‐oligomers and providing a mechanism to understand the function of these proteins.