Sorting of proteins to the vacuoles of plant cells
Article Abstract:
The protein sorting mechanism in plant vacuoles is dependent on the presence of N-linked oligosaccharide chains present in their polypeptide domains. A hydrophobic signal peptide sequence at the N-terminus first directs these proteins to the endoplasmic reticulum where folding, assembly, glycosylation and disulfide bond formation occur. Passage through the Golgi apparutus then occurs with the subsequent modification of their glycan domains. Vacuolar targetting subequently occurs.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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Cross-strand disulphides in cell entry proteins: poised to act
Article Abstract:
Research examines the role of cross-strand disulphide bonds in cell entry events involving entry of proteins such as botulinum neurotoxin and human immunodeficiency virus. Results indicate that the entry of these agents involve cleavage of the cross-strand disulphide bonds. Data show that these bonds possess high potential energy in terms of torsional energy and deformation energy and that they are present in proteins involved in cell entry.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 2004
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Auxin-binding proteins and their possible roles in auxin-mediated plant cell growth
Article Abstract:
Auxin mediates cellular growth and maturation in plants. It promotes cell elongation by inducing plasma membrane hydrogen-adenosine triphosphatase to cause changes in cell wall plasticity and by stimulating messenger ribonucleic acids that promote cell wall stability during expansion. These responses involves multiple auxin receptors located in the endoplasmic reticulum, plasma membrane and nucleus.
Publication Name: BioEssays
Subject: Biological sciences
ISSN: 0265-9247
Year: 1992
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