Amino-Terminal Region of SecA Is Involved in the Function of SecG for Protein Translocation into Escherichia coli Membrane Vesicles

1998 ◽  
Vol 124 (1) ◽  
pp. 122-129 ◽  
Author(s):  
H. Mori ◽  
H. Sugiyama ◽  
M. Yamanaka ◽  
K. Sato ◽  
M. Tagaya ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Translocation ◽  
Membrane Vesicles ◽  
Terminal Region ◽  
Amino Terminal

scholarly journals Characterization of pp60src phosphorylation in vitro in Rous sarcoma virus-transformed cell membranes.

1985 ◽  
Vol 5 (5) ◽  
pp. 916-922 ◽  
Author(s):  
M D Resh ◽  
R L Erikson
Keyword(s):  
Plasma Membrane ◽  
Rous Sarcoma Virus ◽  
Membrane Vesicles ◽  
Terminal Region ◽  
Transformed Cell ◽  
Amino Terminal ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Carboxy Terminal

Phosphorylation of the src gene product pp60v-src was studied in plasma membrane fractions prepared from Rous sarcoma virus-transformed vole cells. Upon addition of [gamma-32P]ATP to isolated membrane vesicles, phosphate was incorporated into a 60,000-dalton polypeptide identified as pp60v-src. In the presence of vanadate, pp60v-src phosphorylation was stimulated ca. 30-fold. At low concentrations of ATP (1 microM), this reaction occurred almost exclusively on the carboxy-terminal 26,000-dalton region of pp60v-src. However, at higher ATP concentrations (100 microM), additional sites of phosphorylation were evident in the amino-terminal 34,000-dalton region. Kinetic analyses, performed under conditions in which ATP hydrolysis was minimal, revealed that the phosphorylation reaction at the carboxy terminus exhibited a higher Vmax and a lower Km for ATP than those occurring at the amino terminus. In addition, the amino-terminal region of pp60v-src was more rapidly dephosphorylated than the carboxy-terminal region. These results indicate that interaction of pp60v-src with the plasma membrane may limit the extent of amino-terminal phosphorylation by lowering the rate of the reaction and the affinity for the substrate while increasing its susceptibility to phosphoprotein phosphatases. We suggest that the use of transformed-cell membrane preparations provides a model system for studying the possible regulatory roles of phosphorylation and dephosphorylation on pp60v-src function.

The Amino Acid Sequence of the N-Terminal Region of Some 30 S Ribosomal Proteins from Escherichia coli and Bacillus stearothermophilus: Homologies in Ribosomal Proteins

1973 ◽  
Vol 51 (8) ◽  
pp. 1215-1217 ◽  
Author(s):  
M. Yaguchi ◽  
C. Roy ◽  
A. T. Matheson ◽  
L. P. Visentin
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Ribosomal Proteins ◽  
Bacillus Stearothermophilus ◽  
Terminal Region ◽  
Amino Terminal

The sequence of the amino terminal region of fifteen 30 S ribosomal proteins from Escherichia coli and three proteins from Bacillus stearothermophilus are compared.

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