TY - JOUR
T1 - Ubiquitin in Chlamydomonas reinhardii Distribution in the cell and effect of heat shock and photoinhibition on its conjugate pattern
AU - WETTERN, Michael
AU - PARAG, Hadas A.
AU - POLLMANN, Lutz
AU - OHAD, Itzhak
AU - KULKA, Richard G.
PY - 1990/8
Y1 - 1990/8
N2 - Ubiquitin, a highly conserved 76‐amino‐acid protein, is involved in the response of many types of eukaryotic cells to stress but little is known about its role in lower plants. In the present study we have investigated the distribution of ubiquitin in the unicellular alga Chlamydomonas reinhardii as well as the effect of heat and light stress on its conjugation to cellular proteins. Immunoelectron microscopy shows that ubiquitin is located in the chloroplast, nucleus, cytoplasm, pyrenoid and on the plasma membrane. The location of ubiquitin within chloroplasts has not been observed previously. In immunoblots of whole cell extracts with an antibody to ubiquitin a prominent conjugate band with an apparent molecular mass of 29 kDa and a broad region of high‐molecular‐mass conjugates (apparent molecular mass > 45 kDa) were observed. Exposure of cells to a 41.5°C heat shock in both the dark and light caused the disappearance of the 29‐kDa conjugate and an increase in the high‐molecular‐mass conjugates. After step down to 25°C the 29‐kDa conjugate reappeared while the levels of high‐molecular‐mass conjugates decreased. In light, the recovery of the 29‐kDa band was more rapid than in the dark. Photoinhibition alters the ubiquitin conjugation pattern similarly to heat shock, but to a lesser degree. These observations imply that, in Chlamydomonas, ubiquitin has a role in the chloroplast and in the response to heat and light stress.
AB - Ubiquitin, a highly conserved 76‐amino‐acid protein, is involved in the response of many types of eukaryotic cells to stress but little is known about its role in lower plants. In the present study we have investigated the distribution of ubiquitin in the unicellular alga Chlamydomonas reinhardii as well as the effect of heat and light stress on its conjugation to cellular proteins. Immunoelectron microscopy shows that ubiquitin is located in the chloroplast, nucleus, cytoplasm, pyrenoid and on the plasma membrane. The location of ubiquitin within chloroplasts has not been observed previously. In immunoblots of whole cell extracts with an antibody to ubiquitin a prominent conjugate band with an apparent molecular mass of 29 kDa and a broad region of high‐molecular‐mass conjugates (apparent molecular mass > 45 kDa) were observed. Exposure of cells to a 41.5°C heat shock in both the dark and light caused the disappearance of the 29‐kDa conjugate and an increase in the high‐molecular‐mass conjugates. After step down to 25°C the 29‐kDa conjugate reappeared while the levels of high‐molecular‐mass conjugates decreased. In light, the recovery of the 29‐kDa band was more rapid than in the dark. Photoinhibition alters the ubiquitin conjugation pattern similarly to heat shock, but to a lesser degree. These observations imply that, in Chlamydomonas, ubiquitin has a role in the chloroplast and in the response to heat and light stress.
UR - http://www.scopus.com/inward/record.url?scp=0025046096&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1990.tb19159.x
DO - 10.1111/j.1432-1033.1990.tb19159.x
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C2 - 2167845
AN - SCOPUS:0025046096
SN - 0014-2956
VL - 191
SP - 571
EP - 576
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 3
ER -