Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein

SecB is a 16-kDa cytosolic chaperone protein that is required for efficient export of particular proteins in Escherichia coli. To identify regions of SecB that contribute to efficient protein export, we isolated secB point mutants that are defective for protein export in vivo. We obtained missense m...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	The Journal of biological chemistry 1993-01, Vol.268 (3), p.1590-1595
Hauptverfasser:	GANNON, P. M, KUMAMOTO, C. A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence ATP-Binding Cassette Transporters Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Base Sequence Biological and medical sciences Carbonyl Cyanide m-Chlorophenyl Hydrazone - pharmacology Carrier Proteins - chemistry Carrier Proteins - metabolism Cell physiology chaperones Escherichia coli Escherichia coli - chemistry Escherichia coli - genetics Escherichia coli Proteins Fundamental and applied biological sciences. Psychology Genes, Bacterial interaction maltose-binding protein Maltose-Binding Proteins Microscopy, Fluorescence Molecular and cellular biology Molecular Sequence Data Monosaccharide Transport Proteins Mutation Protein Folding Protein Precursors - metabolism SecB protein Secretion. Exocytosis Spectrometry, Fluorescence Structure-Activity Relationship
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Schreiben Sie den ersten Kommentar!