SecB Dependence of an Exported Protein Is a Continuum Influenced by the Characteristics of the Signal Peptide or Early Mature Region

Kim, Jin Oh; Luirink, Joen; Kendall, Debra A.

doi:10.1128/jb.182.14.4108-4112.2000

Cited by 9 publications

(16 citation statements)

References 30 publications

(31 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Consistent with this notion, PhoE utilizes a SecB-dependent pathway, yet the PhoE signal sequence has been found to crosslink with SRP upon readdition of wild-type lysate in a heterologous expression system [22] or when Ffh is added to physiological concentration in a homologous expression system [9]. In addition, some of the PhoA signal sequences, which are shown here to be sensitive to Ffh depletion, have also been shown to accumulate in the absence of SecB [12] and SecA [23] in vivo. Collectively, the results indicate that while signal peptide hydrophobicity may in£uence the a¤nity of the preprotein for these components, the substrate speci¢city of the SRP-and SecA/SecB-dependent pathways may overlap.…”

Section: Resultssupporting

confidence: 73%

See 1 more Smart Citation

Is Ffh required for export of secretory proteins?

Kim¹,

Rusch²,

Luirink³

et al. 2001

FEBS Letters

Self Cite

View full text Add to dashboard Cite

In Escherichia coli, protein export from the cytoplasm may occur via the signal recognition particle (SRP)-dependent pathway or the Sec-dependent pathway. Membrane proteins utilize the SRP-dependent route, whereas many secretory proteins use the cytoplasmic Sec machinery. To examine the possibility that signal peptide hydrophobicity governs which targeting route is utilized, we used a series of PhoA signal sequence mutants which vary only by incremental hydrophobicity changes. We show that depletion of SRP, but not trigger factor, affects all the mutants examined. These results suggest secretory proteins with a variety of signal sequences, as well as membrane proteins, require SRP for export. ß

show abstract

Section: Resultssupporting

confidence: 73%

“…C600 and BB4802 (C600 vtig: :kan) (gifts from B. Bukau) were used for the trigger factor studies. The mutant alkaline phosphatase plasmids have been described previously [11,12].…”

Section: Strains and Plasmidsmentioning

confidence: 99%

Is Ffh required for export of secretory proteins?

Kim¹,

Rusch²,

Luirink³

et al. 2001

FEBS Letters

Self Cite

View full text Add to dashboard Cite

show abstract

“…These precursor proteins in complex with SRP could be targeted to SecA with high efficiency even in the absence of SecB. Consistent with this idea, when the hydrophobicity of the signal sequence is increased to optimize Ffh binding, the precursor protein becomes SecB independent, whereas when the hydrophobicity is decreased, the precursor protein becomes SecB dependent (Kim et al 2000). Another possibility is that the SecB-independent proteins are better substrates for other chaperones or SecA itself.…”

Section: Discussionsupporting

confidence: 60%

Sec-dependent protein export and the involvement of the molecular chaperone SecB

Kim

Kendall

2000

Cell Stress Chaper

Self Cite

View full text Add to dashboard Cite

“…Insertion of positive charges in the early mature domain blocks secretion 17 , 21 – 24 and their removal can optimize export 25 . Chaperones such as SecB 23 , 26 – 28 , Trigger Factor 29 and SecA 30 , 31 can specifically recognize mature domains.…”

Section: Introductionmentioning

confidence: 99%

MatureP: prediction of secreted proteins with exclusive information from their mature regions

Orfanoudaki

Markaki

Chatzi

et al. 2017

Sci Rep

View full text Add to dashboard Cite

More than a third of the cellular proteome is non-cytoplasmic. Most secretory proteins use the Sec system for export and are targeted to membranes using signal peptides and mature domains. To specifically analyze bacterial mature domain features, we developed MatureP, a classifier that predicts secretory sequences through features exclusively computed from their mature domains. MatureP was trained using Just Add Data Bio, an automated machine learning tool. Mature domains are predicted efficiently with ~92% success, as measured by the Area Under the Receiver Operating Characteristic Curve (AUC). Predictions were validated using experimental datasets of mutated secretory proteins. The features selected by MatureP reveal prominent differences in amino acid content between secreted and cytoplasmic proteins. Amino-terminal mature domain sequences have enhanced disorder, more hydroxyl and polar residues and less hydrophobics. Cytoplasmic proteins have prominent amino-terminal hydrophobic stretches and charged regions downstream. Presumably, secretory mature domains comprise a distinct protein class. They balance properties that promote the necessary flexibility required for the maintenance of non-folded states during targeting and secretion with the ability of post-secretion folding. These findings provide novel insight in protein trafficking, sorting and folding mechanisms and may benefit protein secretion biotechnology.

show abstract

SecB Dependence of an Exported Protein Is a Continuum Influenced by the Characteristics of the Signal Peptide or Early Mature Region

Cited by 9 publications

References 30 publications

Is Ffh required for export of secretory proteins?

Is Ffh required for export of secretory proteins?

Sec-dependent protein export and the involvement of the molecular chaperone SecB

MatureP: prediction of secreted proteins with exclusive information from their mature regions

Contact Info

Product

Resources

About