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September 2012, Week 2

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Dictybase Northwestern <[log in to unmask]>
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Fri, 14 Sep 2012 21:29:09 +0000
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dictyNews
Electronic Edition
Volume 38, number 23
September 14, 2012

Please submit abstracts of your papers as soon as they have been
accepted for publication by sending them to [log in to unmask]
or by using the form at
http://dictybase.org/db/cgi-bin/dictyBase/abstract_submit.

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=========
Abstracts
=========


Amino acid repeats cause extraordinary coding sequence 
variation in the social amoeba Dictyostelium discoideum

Clea Scala1 *, Xiangjun Tian2 *, Natasha J. Mehdiabadi1,3,, 
Margaret H. Smith1, Gerda Saxer4, Katie Stephens1, 
Prince Buzombo1, Joan E. Strassmann2, David C. Queller2


PLoS One, in press

Protein sequences are normally the most conserved elements 
of genomes owing to purifying selection to maintain their 
functions.  We document an extraordinary amount of 
within-species protein sequence variation in the model 
eukaryote Dictyostelium discoideum stemming from triplet 
DNA repeats coding for long strings of single amino acids.  
D. discoideum has a very large number of such strings, many 
of which are polyglutamine repeats, the same sequence that 
causes various human neurological disorders in humans, like 
Huntington’s disease.  We show here that D. discoideum 
coding repeat loci are highly variable among individuals, making 
D. discoideum a candidate for the most variable proteome.  
The coding repeat loci are not significantly less variable than 
similar non-coding triplet repeats. This pattern is consistent 
with these amino-acid repeats being largely non-functional 
sequences evolving primarily by mutation and drift.


Submitted by David Queller [[log in to unmask]]
---------------------------------------------------------------------------


Mitochondrial fission and fusion in Dictyostelium discoideum: 
a search for proteins involved in membrane dynamics

Brixey G Schimmel, Gregory W Berbusse, and Kari Naylor


BMC Research Notes, in press

Background
Mitochondrial morphology is maintained by two distinct membrane 
events -fission and fusion. Altering these conserved processes can 
disrupt mitochondrial morphology and distribution, thereby 
disrupting the organelle’s functionality and impeding cellular 
function. In higher eukaryotes, these processes are mediated by 
a family of dynamin-related proteins (DRP’s). In the lower 
eukaryotes, for instance Dictyostelium discoideum, mitochondrial 
fission and fusion have been implicated but not yet established. 
To understand the overall mechanism of these dynamics across 
organisms, we developed an assay to identify fission and fusion 
events in Dictyostelium and to assess the involvement of the 
mitochondrial proteins, MidA, CluA, and two DRP’s, DymA 
and DymB.

Findings
Using laser scanning confocal microscopy we show, for the first t
ime, that lower eukaryotes mediate mitochondrial fission and fusion. 
In Dictyostelium, these processes are balanced, occurring 
approximately 1 event/minute. Quantification of the rates in midA-, 
cluA-, dymA-, or dymB- strains established that MidA appears to 
play an indirect role in the regulation of fission and fusion, while the 
DRP’s are not essential for these processes. Rates of fission and 
fusion were significantly reduced in cluA-cells, indicating that CluA 
is necessary for maintaining both fission and fusion.

Conclusions
We have successfully demonstrated that Dictyostelium mitochondria 
undergo the dynamic processes of fission and fusion. The classical 
mediators of membrane dynamics - the DRP’s – are not necessary 
for these dynamics, whereas CluA is necessary for both processes. 
This work contributes to our overall understanding of mitochondrial 
dynamics and ultimately will provide additional insight into 
mitochondrial disease. 


Submitted by Kari Naylor [[log in to unmask]]
==============================================================
[End dictyNews, volume 38, number 23]

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