Copy Link
Add to Bookmark
Report
dictyNews Volume 34 Number 08
dictyNews
Electronic Edition
Volume 34, number 8
March 5, 2010
Please submit abstracts of your papers as soon as they have been
accepted for publication by sending them to dicty@northwestern.edu
or by using the form at
http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit.
Back issues of dictyNews, the Dicty Reference database and other
useful information is available at dictyBase - http://dictybase.org.
Follow dictyBase on twitter:
http://twitter.com/dictybase
=========
Abstracts
=========
Crystal Structure of the Alpha-Kinase Domain of Dictyostelium Myosin
Heavy Chain Kinase A
Qilu Ye*, Scott W. Crawley*, Yidai Yang, Graham P. Côté, and Zongchao Jia
Department of Biochemistry, Queen’s University, Kingston, Ontario,
Canada K7L 3N6.
*These authors contributed equally to this work.
To whom correspondence should be addressed.
E-mail: coteg@queensu.ca
Science Signaling, In press
Dictyostelium discoideum myosin II heavy chain kinase A (MHCK A) disrupts
the assembly and cellular activity of bipolar filaments of myosin II by
phosphorylating sites within its alpha-helical, coiled-coil tail. MHCK A is a
member of the atypical alpha-kinase family of serine and threonine protein
kinases and displays no sequence homology to typical eukaryotic protein
kinases. We report the crystal structure of the alpha-kinase domain (A-CAT)
of MHCK A. When crystallized in the presence of adenosine triphosphate
(ATP), A-CAT contained adenosine monophosphate (AMP) at the active site.
However, when crystallized in the presence of ATP and a peptide substrate,
which does not appear in the structure, adenosine diphosphate (ADP) was
found at the active site and an invariant aspartic acid residue (Asp766) at the
active site was phosphorylated. The aspartylphosphate group was exposed to
the solvent within an active-site pocket that might function as a docking site for
substrates. Access to the aspartylphosphate was regulated by a conformational
switch in a loop that bound to a magnesium ion (Mg2+), providing a mechanism
that allows alpha-kinases to sense and respond to local changes in Mg2+.
Submitted by Scott Crawley [crawleys@queensu.ca]
--------------------------------------------------------------------------------
A flavin-dependent halogenase catalyzes the
chlorination step in the biosynthesis of
Dictyostelium differentiation-inducing factor 1
Christopher S. Neumann (a), Christopher T. Walsh (a), and
Robert R. Kay (b)
(a) Department of Biological Chemistry and Molecular Pharmacology,
Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115;
and (b) Division of Cell Biology, Medical Research Council Laboratory
of Molecular Biology, Hills Road, Cambridge CB2 OQH, UK
Proc Natl Acad Sci USA, in press
Differentiation-inducing factor 1 (DIF-1) is a polyketide-derived
morphogen which drives stalk cell formation in the developmental
cycle of Dictyostelium discoideum. Previous experiments demonstrated
that the biosynthetic pathway proceeds via dichlorination of the precursor
molecule THPH, but the enzyme responsible for this transformation has
eluded characterization. Our recent studies on prokaryotic flavin-dependent
halogenases and insights from the sequenced Dd genome led us to a
candidate gene for this transformation. In this work, we present in vivo and
in vitro evidence that chlA from Dd encodes a flavin-dependent halogenase
capable of catalyzing both chlorinations in the biosynthesis of DIF-1. The
results provide in vitro characterization of a eukaryotic oxygendependent
halogenase and demonstrate a broad reach in biology for this molecular
tailoring strategy, notably its involvement in the differentiation program of
a social amoeba.
Submitted by Christopher S. Neumann [christopher_neumann@hms.harvard.edu]
==============================================================
[End dictyNews, volume 34, number 8]
