Publication Date:
1988-02-26
Description:
Leader peptides that function to direct export of proteins through membranes have some common features but exhibit a remarkable sequence diversity. Thus there is some question whether leader peptides exert their function through conventional stereospecific protein-protein interaction. Here it is shown that the leader peptides retarded the folding of precursor maltose-binding protein and ribose-binding protein from Escherichia coli. This kinetic effect may be crucial in allowing precursors to enter the export pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, S -- Liu, G -- Topping, T B -- Cover, W H -- Randall, L L -- GM29798/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1033-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry/Biophysics Program, Washington State University, Pullman 99164.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3278378" target="_blank"〉PubMed〈/a〉
Keywords:
*ATP-Binding Cassette Transporters
;
Bacterial Proteins/*metabolism
;
Biological Transport
;
Carrier Proteins/metabolism
;
Endopeptidase K
;
Escherichia coli/*metabolism
;
*Escherichia coli Proteins
;
Guanidine
;
Guanidines/pharmacology
;
Kinetics
;
Maltose-Binding Proteins
;
*Monosaccharide Transport Proteins
;
Peptide Hydrolases
;
*Periplasmic Binding Proteins
;
*Protein Conformation/drug effects
;
Protein Denaturation
;
Protein Precursors/*metabolism
;
Protein Sorting Signals/pharmacology/*physiology
;
Serine Endopeptidases/pharmacology
;
Spectrometry, Fluorescence
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
