Parallel Effects of signal Peptide Hydrophobic Core Modifications on Co-translational Translocation and Post-Translational Cleavage by Purified Signal Peptidase

Cioffi, Joseph A.; Allen, Kimberly; Lively, Mark O.; Kemper, Byron

doi:10.1016/s0021-9258(18)63809-8

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Er Signal Sequences2

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1990

2013

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Cited by 25 publications

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“…These sequences are similar to bacterial signal peptides in that they have the n-, h-, and c-domains discussed above. Also, like their bacterial counterparts, the hydrophobic character is important for function as a translocation signal .…”

Section: Er Signal Sequencesmentioning

confidence: 99%

“…Also, like their bacterial counterparts, the hydrophobic character is important for function as a translocation signal. 26 Amazingly, many artificial peptides can function as translocation signals, as demonstrated by Kaiser et al 27 The most important key feature is hydrophobicity above a certain threshold. ER signal peptides have a higher content of leucine residues relative to bacterial signal peptides.…”

Section: Er Signal Sequencesmentioning

confidence: 99%

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Signal Peptidases

et al. 2002

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Section: Er Signal Sequencesmentioning

confidence: 99%

Section: Er Signal Sequencesmentioning

confidence: 99%

Signal Peptidases

et al. 2002

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Targeting of proteins into the eukaryotic secretory pathway: Signal peptide structure/function relationships

Nothwehr

Gordon

1990

BioEssays

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Much progress has been made in recent years regarding the mechanisms of targeting of secretory proteins to, and across, the endoplasmic reticulum (ER) membrane. Many of the cellular components involved in mediating translocation across this bilayer have been identified and characterized. Polypeptide domains of secretory proteins, termed signal peptides, have been shown to be necessary, and in most cases sufficient, for entry of preproteins into the lumen of the ER. These NH2-terminal segments appear to serve multiple roles in targeting and translocation. The structural features which mediate their multiple functions are currently the subject of intense study.

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