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doi:10.1534/genetics.106.069013
A more recent version of this article appeared on March 1, 2007.
REGULAR RESEARCH PAPERS |
Point mutations in the stem region and the fourth AAA domain of cytoplasmic dynein heavy chain partially suppress the phenotype of NUDF/LIS1 loss in Aspergillus nidulans
Lei Zhuang 1, Jun Zhang 1 and Xin Xiang 1*
1 USUHS
* To whom correspondence should be addressed. E-mail: xxiang{at}usuhs.mil.
Submitted on November 29, 2006
Revised on December 29, 2006
Accepted on 4 January 2007
Cytoplasmic dynein performs multiple cellular tasks but its regulation remains unclear. The dynein heavy chain has a N-terminal stem that binds to other subunits and a C-terminal motor unit that contains six AAA (ATPase associated with cellular activities) domains and a microtubule-binding site located between AAA4 and AAA5. In Aspergillus nidulans, NUDF (a LIS1 homolog) functions in the dynein pathway, and two nudF6 partial suppressors were mapped to the nudA dynein heavy chain locus. Here we identified these two mutations. The nudAL1098F mutation resides in the stem region, and nudAR3086C is in the end of AAA4. These mutations partially suppress the phenotype of nudF deletion but do not suppress the phenotype exhibited by mutants of dynein intermediate chain and Arp1. Surprisingly, the stronger 
nudF suppressor, nudAR3086C, causes an obvious decrease in the basal level of dynein's ATPase activity and an increase in dynein's distribution along microtubules. Thus, suppression of the nudF phenotype may be resulted from mechanisms other than simply enhancing dynein’s ATPase activity. The fact that a mutation in the end of AAA4 negatively regulates dynein's ATPase activity but partially compensates for NUDF loss indicates the importance of the AAA4 domain in dynein regulation in vivo.
Key Words: LIS1, Microtubule, NUDF, dynein, mutation
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