Involvement of the nusA and nusB gene products in transcription of Escherichia coli tryptophan operon in vitro

1982 ◽  
Vol 185 (2) ◽  
pp. 369-371 ◽  
Author(s):  
Kazuyuki Kuroki ◽  
Shunsuke Ishii ◽  
Yasunobu Kano ◽  
Tomoyuki Miyashita ◽  
Kayoko Nishi ◽  
...  
1976 ◽  
Vol 103 (2) ◽  
pp. 383-393 ◽  
Author(s):  
Frank Lee ◽  
Catherine L. Squires ◽  
Craig Squires ◽  
Charles Yanofsky

2006 ◽  
Vol 188 (5) ◽  
pp. 1786-1797 ◽  
Author(s):  
Ekaterina N. Andreishcheva ◽  
Willie F. Vann

ABSTRACT Escherichia coli K1 is responsible for 80% of E. coli neonatal meningitis and is a common pathogen in urinary tract infections. Bacteria of this serotype are encapsulated with the α(2-8)-polysialic acid NeuNAc(α2-8), common to several bacterial pathogens. The gene cluster encoding the pathway for synthesis of this polymer is organized into three regions: (i) kpsSCUDEF, (ii) neuDBACES, and (iii) kpsMT. The K1 polysialyltransferase, NeuS, cannot synthesize polysialic acid de novo without other products of the gene cluster. Membranes isolated from strains having the entire K1 gene cluster can synthesize polysialic acid de novo. We designed a series of plasmid constructs containing fragments of regions 1 and 2 in two compatible vectors to determine the minimum number of gene products required for de novo synthesis of the polysialic acid from CMP-NeuNAc in K1 E. coli. We measured the ability of the various combinations of region 1 and 2 fragments to restore polysialyltransferase activity in vitro in the absence of exogenously added polysaccharide acceptor. The products of region 2 genes neuDBACES alone were not sufficient to support de novo synthesis of polysialic acid in vitro. Only membrane fractions harboring NeuES and KpsCS could form sialic polymer in the absence of exogenous acceptor at the concentrations formed by wild-type E. coli K1 membranes. Membrane fractions harboring NeuES and KpsC together could form small quantities of the sialic polymer de novo.


1975 ◽  
Vol 136 (3) ◽  
pp. 199-214 ◽  
Author(s):  
Hans Pannekoek ◽  
William J. Brammar ◽  
Peter H. Pouwels

Genetics ◽  
1980 ◽  
Vol 95 (4) ◽  
pp. 785-795 ◽  
Author(s):  
Daniel S Oppenheim ◽  
Charles Yanofsky

ABSTRACT E. coli trpE polar mutations are 10 times more polar on trpD gene expression than on downstream (trpC, B, or A) gene expression. This effect was shown to be the result of "translational coupling," in which efficient translation of trpD mRNA reqiures efficient translation of the end of trpE mRNA. The trpE-trpD intercistronic punctuation region consists of overlapping stop and start codons, and the trpE and trpD gene products form a functional complex in the cell. In light of these observations and characteristics, several models for the mechanism of translational coupling are considered.


Sign in / Sign up

Export Citation Format

Share Document