Premium
Plasticity of the kinesin‐microtubule interaction is encoded by the motor domain beta‐sheet
Author(s) -
Richard Jessica,
Kim Elizabeth,
Wojcik Edward,
Kim Sunyoung
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.999.1
Subject(s) - kinesin , microtubule , molecular motor , beta sheet , motor protein , biology , computational biology , biophysics , chemistry , protein structure , microbiology and biotechnology , biochemistry
Kinesins have an unanticipated functional breadth via interaction between their motor domain and microtubules (MTs): they move along cytoskeletal tracks in either direction or modify tracks by elongation or depolymerization. Thus, despite conservation of chemistry, structure, and overall sequence, motor domains are specialized in their intra‐ and inter‐molecular interactions. Here, our bioinformatic studies propose an evolutionary history for the functional plasticity of kinesins. Sequence modifications of the central beta‐sheet are ancient events that correlate with the advent of molecular transporters versus MT‐modifying kinesins. By occupying a physical position between the nucleotide‐ and MT‐binding sites, we propose this beta‐sheet allows for cross‐transmission of information. Furthermore, using meta‐analysis of x‐ray structures, we identified two beta‐sheet motifs that tailor motor domain function for either motility or MT‐modification. This functional rewiring of kinesin through beta‐sheet sequence and structure may be a model by which other motors and NTPases can transduce specific intra‐ and interprotein communication. Supported by NIH (GM097350 and GM066328) and Louisiana Board of Regents [NSF‐Pfund‐143].