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In pollen development, a dramatic reorganization of the actin cytoskeleton takes place during the passage of the pollen grain into dormancy and on activation of pollen tube growth. A role for actin-binding proteins is implicated and we report here the identification of a small gene family in maize that encodes actin depolymerizing factor (ADF)-like(More)
The evolution of insect resistance threatens the effectiveness of Bacillus thuringiensis (Bt) toxins that are widely used in sprays and transgenic crops. Resistance to Bt toxins in some insects is linked with mutations that disrupt a toxin-binding cadherin protein. We show that susceptibility to the Bt toxin Cry1Ab was reduced by cadherin gene silencing(More)
To improve the selection phenotype of the expression plasmid pTEX, a Trypanosoma cruzi rDNA (DNA coding for rRNA) gene spacer fragment (806 bp) containing a mapped transcription start point (tsp) was cloned in the vectors pTEX and pTEX-cat, generating the plasmids pRIBOTEX and pRIBOTEX-cat. T. cruzi cultures transiently transfected with pRIBOTEX-cat(More)
PCNA is an auxilliary protein for DNA polymerase delta whose function is to increase both polymerase activity and processivity. We have previously reported the isolation of a maize cDNA clone encoding a homologue of PCNA. Here we report the identification of a second maize PCNA cDNA clone. The nucleic acid sequence of both clones is almost identical in the(More)
We report the isolation and sequence of a maize cDNA clone which encodes a protein homologous to proliferating cell nuclear antigen (PCNA). The deduced amino acid sequence predicts a protein of 263 amino acids in length. The amino acid sequence shares 62% identity with the human PCNA and 95% identity with the rice homologue of PCNA.
Two cDNA clones encoding a protein homologous to ribosomal protein S4 from the protozoan parasite Trypanosoma cruzi were isolated and characterized. Both clones potentially encode for an identical basic protein of 273 amino acids. Sequence comparisons with other species indicate that this protein is highly conserved. Hybridization studies are consistent(More)
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