Rapid inhibition of protein histidine phosphorylation by UV-irradiation in Xanthomonas oryzae pv. oryzae.
Exposure of Xanthomonas oryzae pv. oryzae cells to 254 nm UV radiation resulted in an alteration of protein phosphorylation. Labelling of the phosphohistidine-containing proteins with molecular masses of 81 and 32 kDa, named p81 and p32, was rapidly reduced following UV irradiation in the early exponential cells, but the decrease was not detected in mid-exponential cells. Mitomycin C, a DNA replication inhibitor, and rifampicin, a drug generally used to inhibit RNA synthesis and DNA replication, were also found to reduce the histidyl phosphorylation. However, this alteration of protein phosphorylation was not hindered by chloramphenicol treatment. A possible role for these histidyl phosphoproteins in sensing UV light is proposed.
Huang
H J
HJ
Institute of Botany, Academia Sinica, Taipei, Taiwan.
Lin
S H
SH
Yang
B C
BC
Cheng
C M
CM
Yang
C C
CC
Kuo
T T
TT
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D004249:DNA Damage; D004260:DNA Repair; D004261:DNA Replication / Q000187:drug effects; D004269:DNA, Bacterial / Q000096:biosynthesis; D006639:Histidine / Q000031:analogs & derivatives* / Q000378:metabolism; D007700:Kinetics; D016685:Mitomycin / Q000494:pharmacology; D008970:Molecular Weight; D010750:Phosphoproteins / Q000737:chemistry / Q000378:metabolism* / Q000528:radiation effects; D012293:Rifampin / Q000494:pharmacology; D014466:Ultraviolet Rays; D014974:Xanthomonas / Q000187:drug effects / Q000378:metabolism* / Q000528:radiation effects*
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D010750:Phosphoproteins; D006639:Histidine; D016685:Mitomycin; C005436:phosphohistidine; D012293:Rifampin