Protein targeting to the endoplasmic reticulum in yeast

Stirling, Colin J.

doi:10.1099/13500872-145-5-991

Cited by 13 publications

(7 citation statements)

References 67 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This translocase would differ from the translocase approached post‐translationally via SecB in its exact composition but would share common core elements (SecYEG). A similar specialization of translocase complexes has been observed in Saccharomyces cerevisiae (reviewed in Stirling, 1999). Alternatively, YidC may be recruited specifically at the translocase upon the co‐translational insertion of inner membrane proteins.…”

Section: Discussionsupporting

confidence: 71%

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

Scotti¹,

Urbanus²,

Brunner

et al. 2000

EMBO J

352

420

View full text Add to dashboard Cite

In Escherichia coli, both secretory and inner membrane proteins initially are targeted to the core SecYEG inner membrane translocase. Previous work has also identified the peripherally associated SecA protein as well as the SecD, SecF and YajC inner membrane proteins as components of the translocase. Here, we use a cross‐linking approach to show that hydrophilic portions of a co‐translationally targeted inner membrane protein (FtsQ) are close to SecA and SecY, suggesting that insertion takes place at the SecA/Y interface. The hydrophobic FtsQ signal anchor sequence contacts both lipids and a novel 60 kDa translocase‐associated component that we identify as YidC. YidC is homologous to Saccharomyces cerevisiae Oxa1p, which has been shown to function in a novel export pathway at the mitochondrial inner membrane. We propose that YidC is involved in the insertion of hydrophobic sequences into the lipid bilayer after initial recognition by the SecAYEG translocase.

show abstract

Section: Discussionsupporting

confidence: 71%

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

Scotti¹,

Urbanus²,

Brunner

et al. 2000

EMBO J

352

420

View full text Add to dashboard Cite

show abstract

“…PaSEC61 codes for Sec61p, a protein that in other organisms has been shown to play a crucial role in the insertion of secretory and membrane polypeptides into the ER and that is essential for cell growth (Rapoport et al ., 1999; Stirling, 1999). This ORF includes an intron of 131 bp after the first 10 nucleotides containing all the canonical sequences for processing (T. Ruíz et al ., in preparation).…”

Section: Resultsmentioning

confidence: 99%

Tunable DNA Cleavage by Intercalating Peptidoconjugates

Mahon¹,

Roy²,

Carreon³

et al. 2006

ChemBioChem

View full text Add to dashboard Cite

The properties of a novel family of peptide-based DNA-cleavage agents are described. Examination of the DNA-cleavage activities of a systematic series of peptide-intercalator conjugates revealed trends that show a strong dependence on peptide sequence. Conjugates differing by a single residue displayed reactivities that varied over a wide range. The cleavage activity was modulated by the electrostatic or steric qualities of individual amino acids. Isomeric conjugates that differed in the position of the tether also exhibited different reactivities. The mechanism of DNA cleavage for these compounds was also probed and was determined to involve hydrogen-atom abstraction from the DNA backbone. Previous studies of these compounds indicated that amino acid peroxides were the active agents in the cleavage reaction; in this report, the chemistry underlying the reaction is characterized. The results reported provide insight into how peptide sequences can be manipulated to produce biomimetic compounds.

show abstract

“…This subcomplex comprises the proteins Sec62p, Sec63p, Sec71p and Sec72p (Deshaies et al 1991;Panzner et al 1995). Posttranslational translocation of proteins into the yeast ER proceeds in two distinct steps (reviewed in Rapoport et al 1999 andStirling 1999). The substrate first binds to the Sec complex via its signal sequence.…”

Section: The Bacterial Secyeg Complexmentioning

confidence: 99%

Signal recognition particle-depencent protein targeting, universal to all kingdoms of life

Koch

Moser

Müller

2002

Reviews of Physiology, Biochemistry and Pharmacology

140

101

View full text Add to dashboard Cite

The signal recognition particle (SRP) and its membrane-bound receptor represent a ubiquitous protein-targeting device utilized by organisms as different as bacteria and humans, archaea and plants. The unifying concept of SRP-dependent protein targeting is that SRP binds to signal sequences of newly synthesized proteins as they emerge from the ribosome. In eukaryotes this interaction arrests or retards translation elongation until SRP targets the ribosome-nascent chain complexes via the SRP receptor to the translocation channel. Such channels are present in the endoplasmic reticulum of eukaryotic cells, the thylakoids of chloroplasts, or the plasma membrane of prokaryotes. The minimal functional unit of SRP consists of a signal sequence-recognizing protein and a small RNA. The as yet most complex version is the mammalian SRP whose RNA, together with six proteinaceous subunits, undergo an intricate assembly process. The preferential substrates of SRP possess especially hydrophobic signal sequences. Interactions between SRP and its receptor, the ribosome, the signal sequence, and the target membrane are regulated by GTP hydrolysis. SRP-dependent protein targeting in bacteria and chloroplasts slightly deviate from the canonical mechanism found in eukaryotes. Pro- and eukaryotic cells harbour regulatory mechanisms to prevent a malfunction of the SRP pathway.

show abstract

Protein targeting to the endoplasmic reticulum in yeast

Cited by 13 publications

References 67 publications

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

Tunable DNA Cleavage by Intercalating Peptidoconjugates

Signal recognition particle-depencent protein targeting, universal to all kingdoms of life

Contact Info

Product

Resources

About