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- W2493014802 abstract "Theexportofproteins totheperiplasmic compartment ofbacterial cells ismediated byan amino-terminal signal peptide. After transport, thesignal peptide iscleaved bya processing enzyme,signal peptidase I.A comparison ofthecleavage sites ofmany exported proteins hasidentified a conserved feature ofsmall, uncharged aminoacids atpositions -1and-3relative tothecleavage site. Todetermine experimentally the sequencesrequired forefficient signal peptide cleavage, we simultaneously randomized theaminoacidresidues frompositions -4to+2oftheTEM-1 I-lactamase enzyme toforma library ofrandomsequences.Mutants thatprovide wild-type levels ofampicillin resistance were thenselected fromtherandom-sequence library. The sequencesof15mutantsindicated a biastowards smallaminoacids. TheN-terminal aminoacidsequenceof thematureenzyme was determined fornineofthemutantstoassign thenew -1 and-3 residues. Alanine was present inthe-1position forallnineofthese mutants, strongly supporting theimportance ofalanine at the-1 position. Theaminoacids atthe-3position were muchlessconserved butwere consistent withthe -3rules derived fromsequencecomparisons. Compared withthewildtype, twooftheninemutantshavean altered cleavage position, suggesting that sequenceismore important thanposition forprocessing ofthesignal peptide. Manysecreted proteins inprokaryotes andeukaryotes are synthesized withan amino-terminal extension referred toas thesignal peptide. Thesignal peptide directs protein translocation acrossmembranes andisremovedbya membraneboundsignal peptidase enzyme after transit through themembrane. Thesignal peptide consists ofthree regions: a 1-to5-residue amino-terminal positively charged segment, a10-to15-residue central hydrophobic core,anda 3-to7-residue hydrophilic carboxy-terminal section (28). Thecarboxy-terminal domainis thesiteofsignal peptide cleavage bythesignal peptidase. There aretwoEscherichia coli signal peptidases. Signal peptidaseII processeslipoproteins (10), andsignal peptidase I processesother secretory proteins (4). Sequence comparisons ofmany cleavage sites indicate that there isno strong sequence homology. However, thesites have a common pattern ofsmall aminoacids atthe- 1(Ala, Gly,andSer)and- 3(Ala, Gly, Ser,Val,andIle)residue positions (20,25).Results from site-directed mutagenesis ofthe-1and-3positions support the- 1 and-3 sequencerequirements inferred fromthe sequencecomparisons(7,24). Inaddition tothesequencerequirements at-1and-3,the transition fromthecentral hydrophobic region tothecleavage region (-6to-4)often contains a helix-breaking residue, suchasPro, Ser, orGly. Studies that support theimportance of a helix-breaking residue include mutagenesis experiments in whichaminoacidsubstitutions ofthe-4proline of,B-lactamase andthe-6proline oftheM13procoat were shownto result ininefficient signal peptide processing (11,24).In contrast, signal peptides thatinclude a proline atthe+1" @default.
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- W2493014802 date "1994-01-01" @default.
- W2493014802 modified "2023-09-24" @default.
- W2493014802 title "Selection ofFunctional Signal Peptide Cleavage Sites froma Library ofRandomSequences" @default.
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