Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

Römisch, Karin; Webb, Jane; Herz, Joachim; Prehn, Siegfried; Frank, Rainer; Vingron, Martin; Dobberstein, Bernhard

doi:10.1038/340478a0

Cited by 346 publications

(222 citation statements)

References 27 publications

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“…E. coli SRP has two components: a protein subunit called Ffh (Bernstein et al, 1989;Romisch et al, 1989) and an 114-nucleotide RNA called 4.5S RNA (Poritz et al, 1990). E. coli SR is a single polypeptide molecule called FtsY (Luirink et al, 1994;Miller et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

A fast and efficient procedure to produce scFvs specific for large macromolecular complexes

Doudna

2007

Journal of Immunological Methods

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We have expanded the application of antibody phage display to a new type of antigen: ribonucleoprotein (RNP) complexes. We describe a simple and efficient method for screening antibodies specific for large intact RNPs and individual components. We also describe a fast and easy method to overcome the abundance of amber stop codons in the positive phage clones. The resulting antibodies have been used in ELISA and Western blot analysis.

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Section: Introductionmentioning

confidence: 99%

A fast and efficient procedure to produce scFvs specific for large macromolecular complexes

Doudna

2007

Journal of Immunological Methods

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“…The peptide concentration used was approx. 2.5 mM in water (90% H20, 10% D20) and [1,2]. SRP54 and Ffh are the units which bind directly with 1.5 mM in a mixed solvent of 50% TFE-da (Cambridge Isotope Labthe signal sequences [5,6].…”

Section: Introductionmentioning

confidence: 99%

Structure of a methionine‐rich segment of Escherichia coli Ffh protein

Chi

et al. 1996

FEBS Letters

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. Materials and methods peptide assumes a stable a-helix along most of its length in aqueous TFE solution. It is clear that this segment of Ffh proteinThe Ffh(410-434) peptide was synthesized by the solid-phase methhas a very strong propensity to form a-helical structure, od on a MilliGen 9050 automated peptide synthesizer. The peptide was purified by reverse phase HPLC using a Phenomenex w-porex C8 Key words." Ffh protein; Peptide; NMR; CD; t~-Helix; column (150 mmx l0 mm, 10 gm). Elution was performed with a Translocation linear water-acetonitrile gradient containing 0.1% trifluoroacetic acid. The N-terminal sequence and molecular weight of the purified peptide were determined using an ABI protein sequencer and fast atom bombardment mass spectroscopy (JEOL JMS-HXll0/ll0A), respectively.

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“…The SRP receptor itself consists of a 69-kDa α subunit and a 30-kDa β subunit and resides in the ER membrane. The SRP receptor (α and β) and the 54-kDa subunit of SRP are all GTPases that harness GTP to effect the docking of ribosomes and the transfer of signal sequences (Romisch et al, 1989) (Bacher et al, 1996) (Bacher et al, 1999). TRAM helps order the insertion process (Do et al, 1996) and determines the rate at which nascent chains are exposed to the lumen (Hegde et al, 1998c) as well as their topology (Hegde et al, 1998b).…”

Section: Protein Targeting To the Ermentioning

confidence: 99%

Glycoprotein Folding in the Endoplasmic Reticulum

Benham

Braakman

2000

Critical Reviews in Biochemistry and Molecular Biology

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Our understanding of eukaryotic protein folding in the endoplasmic reticulum has increased enormously over the last 5 years. In this review, we summarize some of the major research themes that have captivated researchers in this field during the last years of the 20th century. We follow the path of a typical protein as it emerges from the ribosome and enters the reticular environment. While many of these events are shared between different polypeptide chains, we highlight some of the numerous differences between proteins, between cell types, and between the chaperones utilized by different ER glycoproteins. Finally, we consider the likely advances in this field as the new century unfolds and we address the prospect of a unified understanding of how protein folding, degradation, and translation are coordinated within a cell.

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Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP–binding domains

Cited by 346 publications

References 27 publications

A fast and efficient procedure to produce scFvs specific for large macromolecular complexes

A fast and efficient procedure to produce scFvs specific for large macromolecular complexes

Structure of a methionine‐rich segment of Escherichia coli Ffh protein

Glycoprotein Folding in the Endoplasmic Reticulum

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