Effects of domesticated-to-wild gene flow on the genetic structure and diversity of wild papaya (Carica papaya L.) in its Mesoamerican diversity area.

Due to the increase in demand for food production worldwide, the cultivation of improved varieties is used as a strategy in order to maximize production. The improved Maradol papaya variety was introduced to the Yucatan Peninsula (YP), Mexico, the Mesoamerican diversity area of papaya, in the 1990s. The domesticated and wild papaya belong to the same species (Carica papaya L.

Consequences of introgression and gene flow on the genetic structure and diversity of Lima bean ( L.) in its Mesoamerican diversity area.

We evaluated the role of gene flow and wild-crop introgression on the structure and genetic diversity of Lima bean () in the Yucatan Peninsula, an important Mesoamerican diversity area for this crop, using a genotyping-by-sequencing approach (15,168 SNP markers) and two scales. At the local scale, STRUCTURE and NGSEP analyses showed predominantly crop-to-wild introgression, but also evidence of a bidirectional gene flow in the two wild-weedy-crop complexes studied (Itzinté and Dzitnup). The ABBA-BABA tests showed a higher introgression in Itzinté (the older complex) than in Dzitnup (the younger one); at the allelic level, the wild-crop introgression in Itzinté was similar in both directions, in Dzitnup it was higher from crop-to-wild; and at the chromosomal level, introgression in Itzinté was from wild-to-crop, whereas in Dzitnup it occured in the opposite direction.

Isolation of cDNA encoding the catalytic site of phosphatidylinositol-specific phospholipase C from Coffea arabica L.: Recombinant expression and peptide purification.

A cDNA encoding the catalytic site of a phosphatidylinositol-specific phospholipase C (PI-PLC) was isolated from Coffea arabica suspension cells. The cDNA (designated CaPLC) encodes a polypeptide of 308 amino acids, containing the catalytic X and Y domains, and has 99% identity to the soybean gene. Recombinant CaPLC protein was expressed in Escherichia coli, purified, and used to produce a polyclonal antibody.