Two-dimensional Gel Electrophoresis of Ribosomal Proteins as a Novel Approach to Bacterial Taxonomy: Application to the GenusArthrobacter

1995 ◽  
Vol 59 (9) ◽  
pp. 1679-1687 ◽  
Author(s):  
Keiko Ochiai ◽  
Isao Kawamoto
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Bacterial Taxonomy ◽  
Two Dimensional Gel Electrophoresis ◽  
Novel Approach

Analysis of Ribosomal Proteins from a Yellow Mutant of Chlamydomonas reinhardii by Two-dimensional Gel Electrophoresis

1979 ◽  
Vol 174 (9) ◽  
pp. 822-830 ◽  
Author(s):  
István Gyurján ◽  
Géza Erdös ◽  
Nadiezda P. Yurina ◽  
Marina S. Turischeva ◽  
Margarita S. Odintsova
Keyword(s):  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Chlamydomonas Reinhardii

scholarly journals Initial Proteome Analysis of Model Microorganism Haemophilus influenzae Strain Rd KW20

2003 ◽  
Vol 185 (15) ◽  
pp. 4593-4602 ◽  
Author(s):  
Eugene Kolker ◽  
Samuel Purvine ◽  
Michael Y. Galperin ◽  
Serg Stolyar ◽  
David R. Goodlett ◽  
...  
Keyword(s):  
Haemophilus Influenzae ◽  
Gel Electrophoresis ◽  
Ribosomal Proteins ◽  
Protein Identification ◽  
Proteome Analysis ◽  
Tandem Mass ◽  
Two Dimensional ◽  
High Confidence ◽  
Two Dimensional Gel Electrophoresis

ABSTRACT The proteome of Haemophilus influenzae strain Rd KW20 was analyzed by liquid chromatography (LC) coupled with ion trap tandem mass spectrometry (MS/MS). This approach does not require a gel electrophoresis step and provides a rapidly developed snapshot of the proteome. In order to gain insight into the central metabolism of H. influenzae, cells were grown microaerobically and anaerobically in a rich medium and soluble and membrane proteins of strain Rd KW20 were proteolyzed with trypsin and directly examined by LC-MS/MS. Several different experimental and computational approaches were utilized to optimize the proteome coverage and to ensure statistically valid protein identification. Approximately 25% of all predicted proteins (open reading frames) of H. influenzae strain Rd KW20 were identified with high confidence, as their component peptides were unambiguously assigned to tandem mass spectra. Approximately 80% of the predicted ribosomal proteins were identified with high confidence, compared to the 33% of the predicted ribosomal proteins detected by previous two-dimensional gel electrophoresis studies. The results obtained in this study are generally consistent with those obtained from computational genome analysis, two-dimensional gel electrophoresis, and whole-genome transposon mutagenesis studies. At least 15 genes originally annotated as conserved hypothetical were found to encode expressed proteins. Two more proteins, previously annotated as predicted coding regions, were detected with high confidence; these proteins also have close homologs in related bacteria. The direct proteomics approach to studying protein expression in vivo reported here is a powerful method that is applicable to proteome analysis of any (micro)organism.

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