Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

Valent, Quido A.; Kendall, Debra A.; High, Stephen; Kusters, Ron; Oudega, Bauke; Luirink, Joen

doi:10.1002/j.1460-2075.1995.tb00236.x

Cited by 264 publications

(266 citation statements)

References 61 publications

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“…It is, therefore, possible that many proteins move into the SecA/SecB pathway from SRP, and that these two pathways are not mutually exclusive. 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.…”

Section: Resultsmentioning

confidence: 74%

Is Ffh required for export of secretory proteins?

Kim¹,

Rusch²,

Luirink³

et al. 2001

FEBS Letters

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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

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Section: Resultsmentioning

confidence: 74%

Is Ffh required for export of secretory proteins?

Kim¹,

Rusch²,

Luirink³

et al. 2001

FEBS Letters

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“…Rather, a major cotranslational interaction has been identified recently with a component known as trigger factor, which has peptidyl prolyl isomerase activity (Stoller et al, 1995;Valent et al, 1995;Hesterkamp et al, 1996). GroEL thus appears to function posttranslationally, binding to polypeptide chains that have been released from the translation machinery or from other components, perhaps including Hsp70 proteins.…”

Section: W a Fenton And Al Honvichmentioning

confidence: 99%

GroEL‐Mediated protein folding

1997

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I. Architecture of GroEL and GroES and the reaction pathwayA. Architecture of the chaperonins B. Reaction pathway of GroEL-GroES-mediated folding 3. 4. 5.Role of hydrophobicity in recognition Homologous proteins with differing recognition-differences in primary structure versus effects on folding Concluding remarksKeywords: chaperonin; GroES; Hsp60; kinetic partitioning; mechanism of action; X-ray structureThe early studies of Anfinsen and co-workers established that the 1973). Under physiologic conditions inside the cell, however, the primary structure of a protein contains all the information necesfolding process for many proteins, particularly those with multisary to direct the native secondary and tertiary fold (Anfinsen, domain structures, is prone to producing a variety of misfolded species and aggregates. Recent studies indicate that a specialized

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“…Moreover, TF was successfully crosslinked to the nascent chains of either presecretory or non-signal sequence bearing proteins [13]. This association of TF to the nascent chains was no longer stable under high salt/puromycin conditions indicating a binding affinity to the translating ribosome.…”

Section: Introductionmentioning

confidence: 99%

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

Stoller¹,

Tradler²,

Rücknagel³

et al. 1996

FEBS Letters

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The 48 kDa trigger factor (TF) of E. coli was shown to be a peptidyl-prolyl cisltrans isomerase (PPIase). Its location on a ribosomal particle is unique among the PPIases described so far, and suggests a role in de novo protein folding. The trigger factor was investigated with regard to a domain carrying the catalytic activity. An enzymatieally active fragment could be isolated after proteolysis by subtifisin. The resulting polypeptide was analysed by N-terminal sequencing and MALDI-TOF mass spectrometry revealing an 11.8 kDa fragment of TF encompassing the amino acid residues Arg-145 to Glu-251. The nucleotide sequence encoding the amino acid residues Met-140 to Ala-250 of the TF was cloned into vector pQE32. After expression in E. coli the resulting His-tagged polypeptide was isolated on an Ni 2+-NTA column. Subsequent digestion with subtifisin and anionexchange chromatography yielded a TF fragment encompassing amino acids Gin-148 to Thr-249. This fragment may represent the catalytic core of TF since PPIase activity with a specificity constant kcat/Km of 1.3 ~1-1 s -l could be demonstrated when using Suc-Ala-Phe-Pro-Phe-NH-Np as a substrate. Moreover, as was observed for the complete, authentic TF the PPIase activity of the fragment was not inhibited by the peptidomacrofide FK506.

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Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

Cited by 264 publications

References 61 publications

Is Ffh required for export of secretory proteins?

Is Ffh required for export of secretory proteins?

GroEL‐Mediated protein folding

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

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