Identifying a cellular mechanism that contributes to clinal variation in thermal tolerance | Print |


 

Lauren Carrington (PhD Candidate), Travis Johnson (PhD Candidate) , Fiona Cockerell (PhD Candidate), Dr. Lea Rako , Jennifer Shirriffs.

 

A mechanism involving protein synthesis

 

We have data that support an intriguing cellular model in Drosophila melanogaster for a mechanism that facilitates differential adaptation to tropical and cool-temperate climates. The model involves molecular variation in the hsr-omega gene that clines latitudinally and influences rates of protein synthesis. Protein synthesis rates in turn affect heat tolerance levels, especially the extent to which heat tolerance is enhanced after a mild heat shock – other traits may also be affected. We are currently attempting to elucidate details of the cellular mechanism using gene knockout mutants and we are measuring several traits and protein synthesis rates in newly acquired field strains collected over a broad latitudinal range. This will allow us to assess modulation of protein synthesis as a mechanism for adaptation to different climatic regions.

 

In this context the function of hsr-omega centres on variation among strains in the level of functional units in the nuclear hsr-omega transcript (omega-n). Lauren Carrington and Travis Johnson demonstrated that lines with high basal levels of omega-n showed lower rates of basal protein synthesis. Reviews of the cellular and molecular genetics of hsr-omega argue that a likely function of the conserved sequence within the omega-n repeats is to bind and ‘inactivate’ small nuclear proteins (and inactivate them to a greater extent after heat induction of omega-n).  These nuclear proteins are thought to be essential for splicing intron-containing pre-mRNA into mature mRNA. If this proves to be correct it provides a logical mechanism by which hsr-omega variation influences rates of protein synthesis – high levels of omega-n lead to a lack of mature mRNA from intron-containing housekeeping genes with the consequent slowing of general protein synthesis. The shutdown of general protein synthesis is an established component of the cellular heat shock response. In this model omega-n would not affect production of the intronless heat shock proteins, such as hsp70, since their mature mRNAs does not involve intron splicing. Hence, increased synthesis of heat shock protein mRNAs after heat shock could proceed. Quantifying the levels of pre-mRNA and mature mRNA of several key genes, both before and after an appropriate heat shock will provide a test of this hypothesis/mechanism.