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DYNLL2 dynein light chain binds to an extended linear motif of myosin 5a tail that has structural plasticity

Bodor, Andrea and Radnai, László and Hetényi, Csaba and Rapali, Péter and Láng, András and Kövér, E. Katalin and Perczel, András and Wahlgren, Y. Weixiao and Katona, Gergely and Nyitray, László (2014) DYNLL2 dynein light chain binds to an extended linear motif of myosin 5a tail that has structural plasticity. BIOCHEMISTRY, 53. pp. 7107-7122. ISSN 0006-2960

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Abstract

LC8 dynein light chains (DYNLL) are conserved homodimeric eukaryotic hub proteins that participate in diverse cellular processes. Among the binding partners of DYNLL2, myosin 5a (myo5a) is a motor protein involved in cargo transport. Here we provide a profound characterization of the DYNLL2 binding motif of myo5a in free and DYNLL2 bound form by using NMR spectroscopy, X-ray crystallography and molecular dynamics simulations. In the free form the DYNLL2 binding region, located in an intrinsically disordered domain of the myo5a tail, has a nascent helical character. The motif becomes structured and folds into a β-strand upon binding to DYNLL2. Despite all differences of the myo5a sequence from the consensus binding motif, it accommodates into the same DYNLL2 binding groove as all other partners do. Interestingly, while the core motif shows similar interaction pattern in the binding groove as seen in other complexes, the flanking residues make several additional contacts, thereby lengthening the binding motif. The N-terminal extension folds back and partially blocks the free edge of the β-sheet formed by the binding motif itself. The C-terminal extension contacts the dimer interface and interacts with symmetry related residues of the second myo5a peptide. The involvement of flanking residues of the core binding site of myo5a could modify the quaternary structure of the full-length myo5a and affect its biological functions. The presented structural data widen our understanding of the diverse partner recognition of DYNLL proteins and provide an example of a Janus-faced linear motif.  

Item Type: Article
Subjects: Q Science / természettudomány > QD Chemistry / kémia
Depositing User: Dóra K. Menyhárd
Date Deposited: 13 Feb 2015 20:49
Last Modified: 31 Dec 2015 00:15
URI: http://real.mtak.hu/id/eprint/21784

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