scholarly journals Chasing Phosphohistidine, an Elusive Sibling in the Phosphoamino Acid Family

2011 ◽  
Vol 7 (1) ◽  
pp. 44-51 ◽  
Author(s):  
Jung-Min Kee ◽  
Tom W. Muir
Keyword(s):  
Phosphoamino Acid

scholarly journals Identification of Phosphotyrosine-Containing Proteins in Untransformed and Rous Sarcoma Virus-Transformed Chicken Embryo Fibroblasts

1982 ◽  
Vol 2 (6) ◽  
pp. 653-665 ◽  
Author(s):  
Ricardo Martinez ◽  
Kenji D. Nakamura ◽  
Michael J. Weber
Keyword(s):  
Protein Kinases ◽  
Rous Sarcoma Virus ◽  
Chicken Embryo ◽  
Cellular Protein ◽  
Transformed Cells ◽  
Phosphoamino Acid ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Embryo Fibroblasts ◽  
Chicken Embryo Fibroblasts

Phosphorylation on tyrosine residues mediated by pp60srcappears to be a primary biochemical event leading to the establishment of the transformed phenotype in Rous sarcoma virus (RSV)-infected cells. To identify the cellular proteins that undergo tyrosine phosphorylation during transformation, a32P-labeled RSV-transformed chicken embryo cell extract was analyzed by electrophoresis on a polyacrylamide gel. After slicing the gel into approximately 60 slices, phosphoamino acid analyses were carried out on the protein recovered from each gel slice. Phosphotyrosine was found in every gel slice, with two major peaks of this phosphoamino acid aroundMr's of 59 and 36 kilodaltons. When the same analysis was performed with cells infected with a transformation-defectivesrcdeletion mutant of RSV (tdNY101), significant and reproducible peaks of phosphotyrosine were found in only 2 of 60 gel slices. These gel slices corresponded toMr's of 42 and 40 kilodaltons. Identical results were obtained with normal uninfected chicken embryo fibroblasts. We conclude from these observations that pp60srcor the combined action of pp60srcand pp60src-activated cellular protein kinases cause the tyrosine-specific phosphorylation of a very large number of cellular polypeptides in RSV-transformed cells. In addition, untransformed cells appear to possess one or more active tyrosine-specific protein kinases which are responsible for the phosphorylation of a limited number of proteins. These proteins are different from the major phosphotyrosine-containing proteins of the transformed cells.

Phosphopeptide Mapping and Phosphoamino Acid Analysis on Cellulose Thin-Layer Plates

Cell Biology ◽  
1994 ◽  
pp. 422-448 ◽  
Author(s):  
Peter van der Geer ◽  
Kunxin Luo ◽  
Bartholomew M. Sefton ◽  
Tony Hunter
Keyword(s):  
Thin Layer ◽  
Phosphoamino Acid ◽  
Phosphoamino Acid Analysis ◽  
Phosphopeptide Mapping

scholarly journals Direct Selection of Monoclonal Phosphospecific Antibodies without Prior Phosphoamino Acid Mapping

2009 ◽  
Vol 284 (31) ◽  
pp. 20791-20795 ◽  
Author(s):  
Ole Vielemeyer ◽  
Hebao Yuan ◽  
Sandrine Moutel ◽  
Rénette Saint-Fort ◽  
Danming Tang ◽  
...  
Keyword(s):  
Direct Selection ◽  
Phosphoamino Acid ◽  
Selection Of

Phosphorylation of spore coat proteins of Dictyostelium discoideum

1983 ◽  
Vol 61 (9) ◽  
pp. 996-1001 ◽  
Author(s):  
Teshome Akalehiywot ◽  
Chi-Hung Siu
Keyword(s):  
Electrophoretic Mobility ◽  
Dictyostelium Discoideum ◽  
Cellular Proteins ◽  
Developmental Cycle ◽  
Spore Coat ◽  
Coat Proteins ◽  
Phosphoamino Acid ◽  
Molecular Weights ◽  
Phosphorylated Proteins ◽  
Spore Coat Proteins

Phosphorylation of cellular proteins was studied during development of Dictyostelium discoideum. In the second half of the developmental cycle, two heavily phosphorylated proteins were observed together with a limited number of minor phosphorylated proteins. The electrophoretic mobility of these two phosphoproteins corresponded to two of the major spore coat glycoproteins, with apparent molecular weights of 103 000 and 80 000. They were found to be externalized and associated with the spore coat during spore formation. Phosphoserine was the predominant phosphoamino acid in both cases. These two phosphoproteins thus serve as excellent markers for the differentiation of prespore cells in D. discoideum.

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