Processing of Escherichia coli alkaline phosphatase: role of the primary structure of the signal peptide cleavage region 1 1Edited by A. R. Fersht

1998 ◽  
Vol 277 (4) ◽  
pp. 859-870 ◽  
Author(s):  
Andrew L Karamyshev ◽  
Zemphyra N Karamysheva ◽  
Andrey V Kajava ◽  
Vladimir N Ksenzenko ◽  
Marina A Nesmeyanova
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Signal Peptide ◽  
Primary Structure ◽  
Peptide Cleavage

scholarly journals Secretion of recombinant ribonuclease T1 into the periplasmic space of Escherichia coli with the aid of the signal peptide of alkaline phosphatase

FEBS Letters ◽  
1990 ◽  
Vol 265 (1-2) ◽  
pp. 71-74 ◽  
Author(s):  
Takao Fujimura ◽  
Toshiki Tanaka ◽  
Kanako Ohara ◽  
Hiroshi Morioka ◽  
Seiichi Uesugi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Signal Peptide ◽  
Periplasmic Space ◽  
Ribonuclease T1

Requirement for signal peptide cleavage of Escherichia coli prolipoprotein

Science ◽  
1983 ◽  
Vol 221 (4605) ◽  
pp. 59-61 ◽  
Author(s):  
S Inouye ◽  
C. Hsu ◽  
K Itakura ◽  
M Inouye
Keyword(s):  
Escherichia Coli ◽  
Signal Peptide ◽  
Peptide Cleavage

scholarly journals SecB Dependence of an Exported Protein Is a Continuum Influenced by the Characteristics of the Signal Peptide or Early Mature Region

2000 ◽  
Vol 182 (14) ◽  
pp. 4108-4112 ◽  
Author(s):  
Jinoh Kim ◽  
Joen Luirink ◽  
Debra A. Kendall
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Signal Peptide ◽  
Transport Process ◽  
Amino Terminal ◽  
Exported Protein ◽  
Terminal Domains

ABSTRACT We have used Escherichia coli alkaline phosphatase to show the interplay among the characteristics of two amino-terminal domains in the preprotein (the signal peptide and the early mature region), the efficiency with which this protein is transported, and its requirement for SecB to accomplish the transport process. The results suggest that although alkaline phosphatase does not normally require SecB for transport, it is inherently able to utilize SecB, and it does so when its ability to interface with the transport machinery is compromised.

scholarly journals Escherichia coli alkaline phosphatase. Relaxation spectra of ligand binding

1972 ◽  
Vol 126 (3) ◽  
pp. 727-738 ◽  
Author(s):  
S. E. Halford
Keyword(s):  
Escherichia Coli ◽  
Alkaline Phosphatase ◽  
Ligand Binding ◽  
Catalytic Mechanism ◽  
Temperature Jump ◽  
Relaxation Spectrum ◽  
Equilibrium Mixture ◽  
Difference Spectroscopy ◽  
Relaxation Spectra

The temperature-jump technique was used to study the binding equilibrium between the Escherichia coli alkaline phosphatase dimer and 2-hydroxy-5-nitrobenzyl phosphonate in 0.1m-tris buffer, pH8.0. Three partially discrete relaxations were observed, two of which could be related to the bimolecular associations of ligand with different conformations of the enzyme and the third to the interconversion of these states. Relaxation spectra were also used to analyse the changes in the mechanism of ligand binding to alkaline phosphatase caused by increase in ionic strength. The relaxation spectrum observed after the addition of Pi to the equilibrium mixture of phosphonate and enzyme was also studied. Difference spectroscopy indicated that both of these ligands were bound to the alkaline phosphatase dimer at the same time. These results are related to the catalytic mechanism of this enzyme, with particular reference to the role of two identical subunits in a dimeric enzyme that exhibits only one active site functioning in catalysis at any given time.

scholarly journals Invertase signal and mature sequence substitutions that delay intercompartmental transport of active enzyme.

1985 ◽  
Vol 100 (5) ◽  
pp. 1664-1675 ◽  
Author(s):  
I Schauer ◽  
S Emr ◽  
C Gross ◽  
R Schekman
Keyword(s):  
Signal Peptide ◽  
Physical Property ◽  
Golgi Body ◽  
Active Enzyme ◽  
Mutant Form ◽  
Coding Region ◽  
Peptide Cleavage ◽  
Yeast Invertase ◽  
Reduced Rate

The role of structural signals in intercompartmental transport has been addressed by the isolation of yeast invertase (SUC2) mutations that cause intracellular accumulation of active enzyme. Two mutations that delay transport of core-glycosylated invertase, but not acid phosphatase, have been mapped in the 5' coding region of SUC2. Both mutations reduce specifically the transport of invertase to a compartment, presumably in the Golgi body, where outer chain carbohydrate is added. Subsequent transport to the cell surface is not similarly delayed. One mutation (SUC2-s1) converts an ala codon to val at position -1 in the signal peptide; the other (SUC2-s2) changes a thr to an ile at position +64 in the mature protein. Mutation s1 results in about a 50-fold reduced rate of invertase transport to the Golgi body which is attributable to defective signal peptide cleavage. While peptide cleavage normally occurs at an ala-ser bond, the s1 mutant form is processed slowly at the adjacent ser-met position giving rise to mature invertase with an N-terminal met residue. s2 mutant invertase is transported about sevenfold more slowly than normal, with no delay in signal peptide cleavage, and no detectable abnormal physical property of the enzyme. This substitution may interfere with the interaction of invertase and a receptor that facilitates transport to the Golgi body.

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