Psychrophilicity of Bacillus psychrosaccharolyticus: a proteomic study.

Psychrophilicity of Gram-positive bacterium, Bacillus psychrosaccharolyticus was investigated in a proteomic approach. One hundred and thirty-one protein spots were analyzed by electrospray ionization-quadrupole-time of flight-tandem mass spectrometry and identified using an unpublished translated contig database as well as a nonredundant Gram-positive bacteria protein database from NCBI because of the lack of a genome sequence of this organism. Results focused on proteomic behavior of cold-response show that global up-regulation of metabolic functions and protective mechanism by stress responses might play a major role in psychrophilicity of B.

Proteome analysis of the responses of Panax ginseng C. A. Meyer leaves to high light: use of electrospray ionization quadrupole-time of flight mass spectrometry and expressed sequence tag data.

We performed comparative proteomic analyses in order to understand the physiological responses of ginseng (Panax ginseng C. A. Meyer) to high light (HL).

Light-induced dephosphorylation of a 65-kDa protein in the cyanobacterium Synechocystis sp. PCC6803.

We found that a 65-kDa protein (p65) of Synechocystis sp. PCC 6803 is dephosphorylated in a light-dependent manner. In darkness, p65 was specifically phosphorylated and then completely dephosphorylated within 2 min upon exposure to high-intensity light.