Studies on common bakers yeast have led to the discovery of what may be a long-sought mechanism in the life cycle of retroviruses, including the human immunodeficiency virus (HIV). Knowing the details of this step in the infection process could help pinpoint targets for new classes of drugs to fight HIV.
In the Jan. 9 issue of the journal Science, Thomas Menees and Zhi Cheng of the University of Missouri-Kansas City describe the formation of a lariat structure with the genetic material of retrovirus-like elements in bakers yeast and subsequent cutting of the lariat by a yeast enzyme. The findings reported in Science and in the December 2003 Journal of Virology are the payoff of a three-year research gamble by Menees and two postdoctoral researchers pursuing host-cell factors in retroviral infections.
In addition to filling a gap in biologists understanding of how retroviruses replicate, it may turn out that similar lariat structures occur elsewhere in healthy cells and play previously unrecognized roles in cellular processes such as gene activation.
David Hart | NSF
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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