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Schlagwörter:
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Zusammenfassung:
The high affinity of certain cellular polyanions for many proteins
(polyanion-binding proteins (PABPs)) has been demonstrated previously. It has
been hypothesized that such polyanions may be involved in protein structure
stabilization, stimulation of folding through chaperone-like activity, and
intra- and extracellular protein transport as well as intracellular
organization. The purpose of the proteomics studies reported here was to seek
evidence for the idea that the nonspecific but high affinity interactions of
PABPs with polyanions have a functional role in intracellular processes.
Utilizing yeast protein arrays and five biotinylated cellular polyanion probes
(actin, tubulin, heparin, heparan sulfate, and DNA), we identified proteins
that interact with these probes and analyzed their structural and amino acid
sequence requirements as well as their predicted functions in the yeast
proteome. We also provide evidence for the existence of a network-like system
for PABPs and their potential roles as critical hubs in intracellular behavior.
This investigation takes a first step toward achieving a better understanding
of the nature of polyanion-protein interactions within cells and introduces an
alternative way of thinking about intracellular organization.
