Preparation for protein separation of an ion-exchange polymeric stationary phase presenting amino acid and amine units through surface graft polymerization

2005 ◽  
Vol 13 (1) ◽  
pp. 39-44 ◽  
Author(s):  
Seong-Ho Choi ◽  
Kwang-Pill Lee ◽  
Chang-Ho Shin

Microbiology ◽  
2010 ◽  
Vol 156 (12) ◽  
pp. 3791-3800 ◽  
Author(s):  
Amy T. Cavanagh ◽  
Pete Chandrangsu ◽  
Karen M. Wassarman

6S RNA is a small, non-coding RNA that interacts directly with σ 70-RNA polymerase and regulates transcription at many σ 70-dependent promoters. Here, we demonstrate that 6S RNA regulates transcription of relA, which encodes a ppGpp synthase. The 6S RNA-dependent regulation of relA expression results in increased ppGpp levels during early stationary phase in cells lacking 6S RNA. These changes in ppGpp levels, although modest, are sufficient to result in altered regulation of transcription from σ 70-dependent promoters sensitive to ppGpp, including those promoting expression of genes involved in amino acid biosynthesis and rRNA. These data place 6S RNA as another player in maintaining appropriate gene expression as cells transition into stationary phase. Independent of this ppGpp-mediated 6S RNA-dependent regulation, we also demonstrate that in later stationary phase, 6S RNA continues to downregulate transcription in general, and specifically at a subset of the amino acid promoters, but through a mechanism that is independent of ppGpp and which we hypothesize is through direct regulation. In addition, 6S RNA-dependent regulation of σ S activity is not mediated through observed changes in ppGpp levels. We suggest a role for 6S RNA in modulating transcription of several global regulators directly, including relA, to downregulate expression of key pathways in response to changing environmental conditions.





1989 ◽  
Vol 26 (11) ◽  
pp. 390 ◽  
Author(s):  
M. A. Fung ◽  
A. F. Drake ◽  
C. F. Simpson ◽  
D. P. Ndiomu ◽  
S. O. Akapo ◽  
...  






1955 ◽  
Vol 102 (4) ◽  
pp. 435-440 ◽  
Author(s):  
Leonard T. Skeggs ◽  
Walton H. Marsh ◽  
Joseph R. Kahn ◽  
Norman P. Shumway

A preparation of hypertensin I was purified by countercurrent distribution and was shown to migrate as a single component in starch blocks at pH 9.3 and 4.2. It had an isoelectric point of 7.7. Quantitative analysis by ion exchange column chromatography showed eight amino acids in approximately unimolar proportion: aspartic, proline, valine, isoleucine, leucine, tyrosine, phenylalanine, and arginine. There were in addition two moles of histidine.



2003 ◽  
Vol 35 (4) ◽  
pp. 379-383 ◽  
Author(s):  
Peng Liu ◽  
Jun Tian ◽  
Weimin Liu ◽  
Qunji Xue


2015 ◽  
Vol 53 ◽  
pp. 150-155 ◽  
Author(s):  
Fengwei Liu ◽  
Xiaoze Jiang ◽  
Shuang Bao ◽  
Ruili Wang ◽  
Bin Sun ◽  
...  


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