Meeting Abstract

P1.30  Thursday, Jan. 3  Comparison of Stress Protein cDNA and Amino Acid Sequences Among Three Megachild Solitary Bees KRUM, C.J.**; SAVITSKY, A.N.*; HRANITZ, J.M.; BRUBAKER, K.D.; BARTHELL, J.F.; YOCUM, G.D.; Bloomsburg University, Bloomsburg, PA; Bloomsburg University, Bloomsburg, PA; Bloomsburg University, Bloomsburg, PA; Bloomsburg University, Bloomsburg, PA; University of Central Oklahoma, OK; USDA Laboratory, Fargo, ND jhranitz@bloomu.edu

Solitary leafcutting bees in the family Megachilidae occupy a diversity of floral and thermal niches. Megachile fidelis, native to California, prefers nests in cool moist riparian zone habitat. In contrast two Old World, invasive solitary bees in California, M. apicalis and M. rotundata, have eurythermal nesting niches using even the hottest microhabitats the Central Valley of California. Bees in this family offer opportunities to study the structure-function relationships of heat shock protein 70 (HSP 70) and heat shock protein 90 (HSP 90), the most important stress proteins in the eukaryotic cytosol, because expression and function of stress proteins are essential to survival. We compared cDNA and translated protein sequences of homologous regions in the ATPase domain of HSP70 and among the three species of Megachile using honey bee (Apis mellifera) sequence as a outgroup. Alignments showed that HSP70 cDNA were most similar between the more distantly related M. fidelis and M. apicalis than the two Old World leafcutting bees were to each other. In contrast, alignments showed that amino acid sequences were most similar between the two closely related leafcutting bee species M. apicalis and M. rotundata. Alignments for HSP 90 showed that cDNA and amino acid sequences were more similar between the two Old World bees compared to the native bee. These results suggest that homologous amino acid HSP70 and HSP 90 sequences in these three solitary bees are maintained by codon usage bias and genetic robustness.