Words similar to brucei
Example sentences for: brucei
How can you use “brucei” in a sentence? Here are some example sentences to help you improve your vocabulary:
Mammalian protein phosphatase 5 (PP5) and its homolog protein phosphatase T1 (Ppt1p) from the yeast Saccharomyces cerevisiae contain a catalytic domain structurally related to the catalytic subunits of PP1, PP2A and PP2B, and an N-terminal domain consisting of multiple tetratricopeptide repeats (TPRs) not found in other members of this family of phosphatases [ 1 2 3 ] . Homologs have also been identified in Xenopus laevis [ 4 ] , Neurospora crassa [ 5 ] , Drosophila melanogaster [ 6 ] , Trypanosoma brucei [ 7 ] , Plasmodium falciparum [ 8 9 ] , and cauliflower [ 10 ] , and homologs for Caenorhabditis elegans, Schizosaccharomyces pombe and Arabidopsis thaliana are predicted (accession number CAB60937, CAA17690 and AAD21727, respectively).
Trypanosoma brucei
Calflagins are flagellar Ca 2+-binding proteins found in Trypanosoma cruzi and T. brucei that have motifs similar to EF-hands.
Interestingly, a recent report about the protein composition of the nuclear envelope of the highly divergent eukaryote Trypanosoma brucei has identified a coiled-coil nuclear envelope protein (TbNUP-1) in this organism that also has no similarity with lamins [ 40 ] . TbNUP-1 is a 350 kDa protein with a striking repeat structure.
Protein phosphatase 5 has been implicated in the control of cell proliferation, in hormonal signal transduction, and in hsp90 chaperone function [ 3 11 12 13 14 15 16 17 ] . However little is known about the regulation of PP5 or its specific role in these pathways, and only one physiological substrate for PP5 has been identified to date, the apoptosis signaling kinase ASK 1 [ 13 ] . PP5 can be activated by lipid in vitro , and removal of the TPR domain or the C terminus generates an active, lipid insensitive form of the enzyme [ 18 19 20 21 ] . PP5 phosphatase activity is also altered by hCRY2 and a fragment of hsp90 in vitro [ 21 22 ] . These findings suggest that PP5 may be autoinhibited and that the binding of protein partners or lipids to the TPR domain could potentially control PP5 activity in cells, however no reports have yet documented how PP5 is regulated in vivo . The activity of PP5 homologs from cauliflower, T. brucei and P. falciparum is stimulated by polyunsaturated fatty acids in vitro [ 7 8 9 10 ] and removal of the TPR domain from P. falciparum PP5 increases activity to the same extent as lipid treatment [ 8 9 ] . This suggests that the TPR domain plays a similar inhibitory role for all PP5 homologs.
Loading...