Document Detail

Topography of the insertion of LamB protein into the outer membrane of Escherichia coli wild-type and lac-lamB cells.
MedLine Citation:
PMID:  6086567     Owner:  NLM     Status:  MEDLINE    
The appearance of newly induced LamB protein at the cell surface of Escherichia coli was followed topographically by immuno-electron microscopy. LamB protein was induced in E. coli wild-type or lac-lamB cells for a short period of time (4 to 6 min), such that the overall level of LamB protein in induced cells was at least twofold higher than that in uninduced cells. Antibodies bound to LamB protein exposed at the cell surface were labeled with a protein A-gold probe, and the probe distribution in briefly induced cells was compared to that in uninduced cells. Analysis of large numbers of cells showed that newly inserted LamB protein appeared homogeneously over the entire cell surface, both in wild-type cells and in lac-lamB cells. A peak of insertion which was observed at the division site of the cell was also observed in the absence of induction and in control experiments in which a nonspecific probe was used. It is concluded therefore that insertion of LamB protein into the cell envelope of E. coli occurs at multiple sites over the entire cell surface. The average amount of LamB protein which appeared at the cell surface after induction was determined for various cell size classes. It was found that cells of various size classes all synthesized LamB protein after induction, indicating that synthesis of the protein was not restricted to cells in a particular stage of the cell cycle. However, the rate of LamB synthesis was found to vary during the cell cycle: this rate was constant regardless of cell size in nondividing cells, whereas it increased in dividing cells. It is concluded that the accumulation of newly induced LamB protein follows a linear pattern.
G H Vos-Scheperkeuter; E Pas; G J Brakenhoff; N Nanninga; B Witholt
Related Documents :
18623357 - Preparation and in vitro analysis of microencapsulated genetically engineered e. coli d...
40957 - Sucrose transport by the escherichia coli lactose carrier.
3911897 - X-ray microanalytic method for measurement of dry matter and elemental content of indiv...
17725227 - Of the morphogenes that make a ring, a rod and a sphere in escherichia coli.
24798977 - Lox/cox inhibitors enhance the antineoplastic effects of all-trans retinoic acid in ost...
7738787 - Thermally-induced cell lysis in escherichia coli k12.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of bacteriology     Volume:  159     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  1984 Aug 
Date Detail:
Created Date:  1984-09-17     Completed Date:  1984-09-17     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  440-7     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Bacterial Outer Membrane Proteins
Bacteriophage lambda / metabolism*
Cell Membrane / metabolism
DNA Transposable Elements*
Escherichia coli / genetics*,  metabolism
Lac Operon*
Receptors, Virus / analysis,  genetics*
Species Specificity
Reg. No./Substance:
0/Bacterial Outer Membrane Proteins; 0/DNA Transposable Elements; 0/Porins; 0/Receptors, Virus; 0/maltoporins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  Plasma cyclic AMP and cyclic GMP in childhood-onset psychoses.
Next Document:  Aspartate-specific peptidases in Salmonella typhimurium: mutants deficient in peptidase E.