Arrest of cytochrome-c oxidase synthesis coordinated with catabolic arrest in dormant Artemia embryos.
We have examined cytochrome-c oxidase (COX) biosynthesis in brine shrimp (Artemia franciscana) embryos during preemergence development (PED), as well as its inhibition under anaerobic dormancy, to determine whether transitions in intracellular pH (pHi) have a regulatory influence on anabolic processes. Under control aerobic conditions (embryo pHi greater than or equal to 7.9), incorporation of radiolabeled amino acids shows that substantial biosynthesis of COX occurs during 12 h of PED (500% increase when corrected for enzyme turnover). This anabolic process is blocked under anoxia, a condition known to foster intracellular acidification (pHi less than or equal to 6.8). The arrest of COX synthesis is quantitatively identical when embryos are incubated aerobically during artifical acidification with CO2 (pHi = 6.8). The data suggest that pHi, directly or indirectly, is a regulator of protein synthesis in Artemia embryos during anaerobic dormancy. Previous work has established a fundamental role for pHi in the arrest of carbohydrate catabolism under anoxia. Thus there appears to be a coordinated suppression of energy-producing and energy-utilizing events as Artemia embryos enter quiescence that involves pHi as the common intracellular signal.
Hofmann
G E
GE
Department of Environmental, Population and Organismic Biology, University of Colorado, Boulder 80309-0334.
Hand
S C
SC
D000143:Acids / Q000494:pharmacology; D000332:Aerobiosis; D000818:Animals; D001156:Artemia / Q000196:embryology* / Q000378:metabolism; D003576:Electron Transport Complex IV / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism; D004625:Embryo, Nonmammalian / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D012146:Rest
D000143:Acids; D003576:Electron Transport Complex IV