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Example sentences for: prl
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The signal sequence is crucial for efficient translocation; mutations in the signal sequence significantly reduce export of the preprotein and complete deletions of the signal sequence eliminate essentially all export [ 5 6 7 8 ] . Selection for extragenic suppressors of such export defective preproteins led to the identification of the prl alleles of secY ( prlA ), secE ( prlG ), secA ( prlD ), and more recently secG ( prlH ) [ 6 9 10 11 ] . Early hypotheses predicted that the Prl suppressors function by expanded or altered interactions with signal sequences, facilitating recognition of mutant as well as wild type signal sequences [ 6 ] .
It has been suggested that perhaps cytoplasmic proteins are not exported in prl suppressor strains because they fold rapidly and escape recognition by SecB, while secretory proteins, even those lacking a signal sequence, fold more slowly, allowing time for SecB recognition and binding [ 5 13 ] . SecB binds to a variety of unfolded proteins in vitro [ 24 25 ] , although binding appears to be more selective in vivo [ 26 ] . This selectivity may be based on the slower folding characteristics of secretory proteins.
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 ] .
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.
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.
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