Determining the conductance of the SecY protein translocation channel for small molecules.

Determining the conductance of the SecY protein translocation channel for small molecules. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Determining the conductance of the SecY protein translocation channel for small molecules. Abstract Text:

Sapar M Saparov,Karl Erlandson,Kurt Cannon,Julia Schaletzky,Sol Schulman,Tom A Rapoport,Peter Pohl,

The channel formed by the SecY complex must maintain the membrane barrier for ions and other small molecules during the translocation of membrane or secretory proteins. We have tested the permeability of the channel by using planar bilayers containing reconstituted purified E. coli SecY complex. Wild-type SecY complex did not show any conductance for ions or water. Deletion of the "plug," a short helix normally located in the center of the SecY complex, or modification of a cysteine introduced into the plug resulted in transient channel openings; a similar effect was seen with a mutation in the pore ring, a constriction in the center of the channel. Permanent channel opening occurred when the plug was moved out of the way by disulfide-bridge formation. These data show that the resting channel on its own forms a barrier for small molecules, with both the pore ring and the plug required for the seal; channel opening requires movement of the plug.

Determining the conductance of the SecY protein translocation channel for small molecules. Publishing Authors By Initials

SM Saparov,K Erlandson,K Cannon,J Schaletzky,S Schulman,TA Rapoport,P Pohl,

For similar genetic processes: mutagenesis: sequence deletion research abstracts see: genetic processes: mutagenesis: sequence deletion research

PUBMED ID PMID:

MEDLINE DATE:

Determining the conductance of the SecY protein translocation channel for small molecules. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Molecular cell

VOLUME: 26

Page Numbers: 501-9

Journal Abbreviation: Mol. Cell

ISSN: 1097-2765

DAY: 25

MONTH: May

YEAR: 2007

Determining the conductance of the SecY protein translocation channel for small molecules. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 9802571

Determining the conductance of the SecY protein translocation channel for small molecules. Keywords Mesh Terms:

KEYWORDS: Sequence Deletion

MESH TERMS: metabolism

Chemical & Substance for Abstract: Determining the conductance of the SecY protein translocation channel for small molecules. Information

Substance Name: SecY protein, E coli

Registry Number: 0

Grant and Affiliation Information for Determining the conductance of the SecY protein translocation channel for small molecules.

AFFILIATION: Institut fuer Biophysik, Johannes Kepler Universitaet Linz, Linz, Austria.

Country: United States

AGENCY: United States NIGMS

GRANT: GM052586

ACRONYM: GM

MEDLINETA: Mol Cell

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Determining the conductance of the SecY protein translocation channel for small molecules Related Publications

• A low-cost high-definition wireless sensor system utilizing intersymbol interference.
• An ultrahigh vacuum fast-scanning and variable temperature scanning tunneling microscope for large scale imaging.
• CT colonography versus colonoscopy for the detection of advanced neoplasia.
• Characterization of the growth behavior of Leishmania tarentolae: a new expression system for recombinant proteins.
• Comparison between BAW and SAW sensor principles.
• Crystal structure and function of the zinc uptake regulator FurB from Mycobacterium tuberculosis.
• Determining the conductance of the SecY protein translocation channel for small molecules.
• Diagnosing paediatric multiple sclerosis versus acute disseminated encephalomyelitis.
• Discovery of the archaeal chemical link between glycogen (starch) synthase families using a new mass spectrometry assay.
• Electromechanical-assisted training for walking after stroke.
• Electron-temperature evolution in expanding ultracold neutral plasmas.
• Fluorous-based carbohydrate microarrays.
• Lentiviral-mediated targeted transgene expression in dorsal spinal cord glia: Tool for the study of glial cell implication in mechanisms underlying chronic pain development.
• Malignant melanoma following scalp irradiation for tinea capitis.
• Modes of administration of antibiotics for symptomatic severe urinary tract infections.
• Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.
• One-step synthesis of labeled sugar nucleotides for protein O-GlcNAc modification studies by chemical function analysis of an archaeal protein.
• Pilot Scale Axenic Mass Cultivation of Microalgae II. Sterols of Blue-Green Algae (Cyanobacteria).
• Steady-state fluorescence polarization in planar lipid membranes Experimental and theoretical analysis of the fluorophores 8-anilino-1-naphthalenesulfonate, 1,6-Diphenyl-1,3,5-hexatriene, dansyllysine-valinomycin and n-(9-anthroyloxy) fatty acids.
• Surprising bacterial nucleotidyltransferase selectivity in the conversion of carbaglucose-1-phosphate.
• Syntheses of pyrimidine acyclic nucleoside phosphonates as potent inhibitors of thymidine phosphorylase (PD-ECGF) from SD-lymphoma.
• [A SIMPLIFIED ELUTION METHOD FOR QUANTITATIVE PAPER CHROMATOGRAPHIC ANALYSIS.]
• [Complications in supervoltage therapy of uterine malignancies]
• [Not Available.]
• [Not Available.]
• [Not Available.]
• [Not Available.]
• [Polyhydramnios, prematurity, dystrophy, polyuria, constipation, nephrocalcinosis and renal tumor: presentation of a classic tubulopathy.]
• [The diagnosis of cold nodules in endemic goiters by means of thin needle biopsy and cytological analysis]
• [Utero-abdominal fistula, a contribution to the question of uterus rupture.]