Words similar to prl
Example sentences for: prl
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Although prlA and prlG strains export secretory proteins that completely lack a signal sequence, there is no evidence of export of any cytoplasmic proteins in a prl suppressor strain [ 13 ] . That is, proteins that are supposed to remain in the cytoplasm are not mislocalized to the periplasm.
Several groups of Arabidopsis mutants that are resistant to the inhibitory effects of high sugar concentrations have been isolated [ 46 47 48 49 50 ] . Characterization of these mutants reveals that the sis5 [ 46 ] , sun6 [ 50 ] , gin6 [ 49 ] and isi3 [ 45 ] mutants are allelic to the abscisic acid insensitive mutant abi4 [ 51 ] and the sis4 [ 46 ] , isi4 [ 45 ] and gin1 [ 45 ] mutants are allelic to the abscisic acid biosynthesis mutant aba2 [ 52 ] . In addition, the ethylene constitutive response mutant ctr1-1 [ 53 ] , as well as the ethylene-overproduction mutant eto1 [ 54 ] , display sugar-resistant phenotypes [ 48 ] . Conversely, the sugar-response mutant sis1 exhibits an ethylene constitutive response phenotype and is allelic to ctr1-1 [ 47 ] . The prl1 mutant, which exhibits increased sensitivity to exogenous sugars [ 55 56 ] , carries a mutation in a gene that encodes a WD protein that interacts with SNF1 protein kinases [ 57 ] .
More recent observations support an alternative mechanism of action for the PrlA/SecY and PrlG/SecE suppressors [ 8 12 ] . First, PrlA/G-mediated suppression does not exhibit allele specificity; all prlA and all prlG alleles that have been examined suppress all signal sequence mutations, implying that suppression is not due to a specific altered interaction that allows recognition of a mutant signal sequence [ 8 12 ] . Furthermore, all of the prlA and prlG alleles suppress complete deletions of the signal sequence, suggesting that an interaction between the signal sequence and the Prl suppressor is not necessary for suppression or even for export [ 5 8 13 ] . Based on these observations, it was proposed that the PrlA and PrlG suppressors do not function through altered interactions with signal sequences, but rather by loss of recognition [ 8 12 ] . The wild type SecE and SecY proteins are thought to function in concert to proofread the signal sequence of secretory proteins, rejecting defective precursors from the export pathway.
There were two reasonable explanations for this unexpected finding; 1) an unfolded state is not sufficient for SecB binding, or 2) SecB binding is not sufficient to promote export in a prl suppressor strain.
In a Prl suppressor strain, however, the proofreading function would be compromised and the mutant protein would be exported [ 8 ] . In the experiments described here, we tested this hypothesis by examining the export of such a cytoplasmic protein with a folding mutation.
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