GLORIA — GEOMAR Library Ocean Research Information Access

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Stimulation of Acanthamoeba actomyosin ATPase activity by myosin-II polymerization (1984)

Kiehart, Daniel P. ; Pollard, Thomas D.

[s.l.] : Nature Publishing Group

Nature 308 (1984), S. 864-866

add to mindlist on the mindlist

Details

ISSN: 1476-4687

Source: Nature Archives 1869 - 2009

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Notes: [Auszug] Acanthamoeba myosin-II was purified and treated with acid phosphatase to decrease the heavy-chain phosphate level to about 0.8 phosphates per myosin molecule14,15. Myosin-II forms bipolar filaments of two different sizes depending on the solution conditions15. In 0-150 mM KC1 with divalent cation ...

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1038/308864a0

Permalink

	Location	Call Number	Limitation	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Essential light chain of Drosophila nonmuscle myosin II (1995)

Edwards, Kevin A. ; Chang, Xiao-Jia ; Kiehart, Daniel P.

Springer

Journal of muscle research and cell motility 16 (1995), S. 491-498

add to mindlist on the mindlist

Details

ISSN: 1573-2657

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary We have cloned and sequenced a cDNA encoding the essential (alkaline) light chain of nonmuscle myosin from Drosophila melanogaster. The protein predicted from the cDNA matches partial amino acid sequence derived from essential light chain protein that copurifies with native nonmuscle myosin heavy chain. This completes the sequence of the three myosin subunits, two of which have been shown genetically to be required for morphogenesis and cytokinesis (the heavy chain encoded by zipper and the regulatory light chain encoded by spaghetti squash). The essential light chain protein is 147 amino acids in length and is 53% identical to human smooth muscle essential light chain. The sequence is consistent with the presence of four helix-loop-helix domains seen in crystallographic structures of the striated muscle myosin light chains and their close relative, calmodulin. We identified the most conserved residues among essential light chain sequences from multiple phyla and present their locations on the crystallographic structure of striated muscle essential light chain. This highlights several conserved contacts among the myosin subunits that may be important for the structure and regulation of the myosin motor. The gene encoding Drosophila nonmuscle essential light chain (Mlc-c) localizes to cytological position 5A6 and we discuss prospects for genetic analysis in this region.