Words similar to prl
Example sentences for: prl
How can you use “prl” in a sentence? Here are some example sentences to help you improve your vocabulary:
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.
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.
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.
The hypothesis driving the present studies was premised on the observation that prl suppressor strains are able to correctly identify secretory proteins, even in the absence of a signal sequence.
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.
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