ABSTRACT
Potato virus X (PVX) encodes three movement proteins, TGBp1, TGBp2 and TGBp3. The 8 kDa TGBp3 is a membrane-embedded protein that has an N-terminal hydrophobic sequence segment and a hydrophilic C terminus. TGBp3 mutants with deletions in the C-terminal hydrophilic region retain the ability to be targeted to cell peripheral structures and to support limited PVX cell-to-cell movement, suggesting that the basic TGBp3 functions are associated with its N-terminal transmembrane region. Fusion of green fluorescent protein to the TGBp3 N terminus abrogates protein activities in intracellular trafficking and virus movement. The intracellular transport of TGBp3 from sites of its synthesis in the rough endoplasmic reticulum (ER) to ER-derived peripheral bodies involves a non-conventional COPII-independent pathway. However, integrity of the C-terminal hydrophilic sequence is required for entrance to this non-canonical route.
Subject(s)
Potexvirus/metabolism , Viral Proteins/metabolism , Biological Transport , Endoplasmic Reticulum/metabolism , Hydrophobic and Hydrophilic Interactions , Molecular Weight , Mutation , Potexvirus/genetics , Viral Proteins/chemistry , Viral Proteins/geneticsABSTRACT
The visual system of microchiropteran bats is usually considered of minor function, but reliable experimental studies are rare. In this paper the visual acuity of three (1 female, 2 male male) vampire bats (Desmodus rotundus) has been investigated in a two-choice training apparatus (striped patterns vs. gray patterns) for light intensities from 0.04 1x to 310 1x. There was a logarithmic dependence between light intensity and visual acuity. The lowest visual angle at 0.04 1x was 2 degrees 31', at 310 1x the minimum resolvable stripe width was 48'.
