Effect of CO<sub>2</sub> Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in <i>Chlamydomonas reinhardtii</i>

Bailly, J; Coleman, John R.

doi:10.1104/pp.87.4.833

Cited by 61 publications

(53 citation statements)

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“…The observed pattern of CA transcript abundance upon exposure to air levels of CO2 is quite similar to the induction pattern observed by Bailly and Coleman (3) in C. reinhardtii 2137 mt+ although they reported that mRNA abundance reached its maximum not after 2 but after 3 h exposure to air. However, the length of the CA transcript they reported is shorter (1.4 kb) than the presently observed 2.0-kb CA Figure 8.…”

Section: Effects Of Transcription Inhibitors On Ca Mrna Accumulation supporting

confidence: 64%

“…Results in Figure 2 showed an increase in the accumulation of the 37-kD CA monomer 2 h after transfer to low-CO2 condition. The 37-kD protein is generally a broadband, which on some occasions can be resolved as a doublet signal of approximately 36 to 37 kD as previously reported (3,6). It is noteworthy that in the Western blots presented here, except for the 37-kD band no other immunosignals were observed indicating the specificity of the affinity-purified antibody against CA.…”

Section: Effect Of Light On Ca Protein Accumulation During Air Adaptasupporting

confidence: 47%

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Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Dionisio-Sese¹,

Fukuzawa²,

Miyachi³

1990

Plant Physiol.

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Section: Effects Of Transcription Inhibitors On Ca Mrna Accumulation supporting

confidence: 64%

Section: Effect Of Light On Ca Protein Accumulation During Air Adaptasupporting

confidence: 47%

Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Dionisio-Sese¹,

Fukuzawa²,

Miyachi³

1990

Plant Physiol.

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“…The effect of light in CA induction may be dependent or independent of the photosynthetic process, and this effect may occur at the post-transcriptional or transcriptional step (6,36). Blue light caused a twofold increase of CA activity in Chlamydomonas reinhardtii (11,35).…”

Section: Discussionmentioning

confidence: 99%

Extra and intracelular activities of carbonic anhydrase of the marine microalga Tetraselmis gracilis (Chlorophyta)

Rigobello-Masini¹,

Aidar²,

Masini³

2003

Braz. J. Microbiol.

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The activities of extra and intracellular carbonic anhydrases (CA) were studied in the microalgae Tetraselmis gracilis (Kylin) Butcher (Chlorophyta, Prasinophyceae) growing in laboratory cultivation. During ten days of batch cultivation, daily determinations of pH, cell number, enzymatic activity, and total dissolved inorganic carbon (DIC), as well as its main species, CO2 and HCO3 -, were performed. Enzymatic activity increased as the growing cell population depleted inorganic carbon from the medium. Carbon dioxide concentration decreased quickly, especially in the third day of cultivation, when a significant increase of the intracellular enzymatic activity was observed. Bicarbonate concentration had its largest decrease in the cultivation medium in the fourth day, when the activity of the extracellular enzyme had its largest increase, suggesting its use by the alga through CA activity. After the fourth cultivation day, half of the cultures were aerated with CO2-free atmospheric air, which caused an increase in the total and external activity of the enzyme, although, in this condition, the stationary growth phase began earlier than in cultures aerated with atmospheric air. The pH of the media was measured daily, increasing from the first to the fourth day, and remaining almost constant until the end of the cultivation. Algal material transferred to the dark lost all enzymatic activity.

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“…It is possible that one or more of these proteins could be involved with the transport mechanism, since neither the nature ofthe transporter nor its location has been determined. Along with noting a transitory decline in the synthesis of certain polypeptides such as the rubisco subunits during the induction phase, Bailly and Coleman (2) reported the transitory synthesis of 49 and 52 kD soluble polypeptides and the prolonged synthesis ofa 20 kD soluble polypeptide in addition to the 37 kD periplasmic carbonic anhydrase. Manuel and Moroney (10) have reported polypeptides ofsimilar molecular mass (20, 37, 44, and 46 kD) which they found to be heavily labeled during the induction phase in crude cell homogenates.…”

mentioning

confidence: 99%

A 36 Kilodalton Limiting-CO₂ Induced Polypeptide of Chlamydomonas Is Distinct from the 37 Kilodalton Periplasmic Carbonic Anhydrase

Geraghty¹,

Anderson²,

Spalding³

1990

Plant Physiol.

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Chiamydomonas reinhardtii possesses a C02-concentrating mechanism, induced by limiting C02, which involves active transport and accumulation of inorganic carbon within the cell. Synthesis of several proteins is induced by limiting CO2, but, of those, only periplasmic carbonic anhydrase has an identified function in the system. No proteins involved in active transport have yet been identified, but induced, membrane-associated polypeptides, such as the 36 kilodalton polypeptide focused on in this paper, would seem to be candidates for such involvement. The 36 kilodalton polypeptide was shown to be synthesized de novo upon transfer of cells to limiting CO2. It was purified using SDS-PAGE and used to produce polyclonal antibodies. Antibodies were used to confirm the air-specific nature of the polypeptide, its strict association with membrane fractions, and the time course of its induction. Using the antibodies, a single, 36 kilodalton polypeptide was found to be specifically immunoprecipitated from in vitro translation products of poly(A @) RNA from cells only after exposure to limiting CO2. The absence of translatable mRNA for this polypeptide in C02-enriched cells indicated that regulation occurs at the level of message abundance. The antibodies were also used to demonstrate the distinction between the limiting-CO2 induced 36 kilodalton polypeptide and the similarly sized, limiting-CO2 induced periplasmic carbonic anhydrase.Chiamydomonas reinhardtii, as well as several other green microalgae and cyanobacteria, exhibit a C02-concentrating system induced by low external levels of C02. This system (reviewed in 1, 13, and 15), which gives them a high apparent affinity for CO2, results from the active transport of inorganic carbon (C1)2. air-adapted cells), their apparent affinity for C02 is much higher than that of C02-enriched cells.Components of the C02-concentrating mechanism include a mechanism for active transport of C1, an internal carbonic anhydrase, and a periplasmic carbonic anhydrase (1, 15). Induction of the C02-concentrating mechanism and periplasmic carbonic anhydrase occur in response to low external Ci. Lack of induction in the presence of CHI indicates that de novo protein synthesis is essential (5, 12, 17). Translation of one or more proteins involved in the system must be initiated or upregulated.The best-characterized protein for which specific involvement in the system and a function have been identified is the periplasmic carbonic anhydrase. Coleman et al. (6) identified a soluble 37 kD polypeptide as the periplasmic carbonic anhydrase in Chlamydomonas. The polypeptide appears following transfer of C02-enriched cells to air conditions. It is excreted into the medium by the CW15 mutant which lacks a normal cell wall.The synthesis of other polypeptides has been correlated with the induction of the C02-concentrating mechanism, but so far none have been assigned a specific function or location. It is possible that one or more of these proteins could be involved with the transport mechanism, si...

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Effect of CO₂ Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Cited by 61 publications

References 18 publications

Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Extra and intracelular activities of carbonic anhydrase of the marine microalga Tetraselmis gracilis (Chlorophyta)

A 36 Kilodalton Limiting-CO₂ Induced Polypeptide of Chlamydomonas Is Distinct from the 37 Kilodalton Periplasmic Carbonic Anhydrase

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Effect of CO2 Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Cited by 61 publications

References 18 publications

Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Light-Induced Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

Extra and intracelular activities of carbonic anhydrase of the marine microalga Tetraselmis gracilis (Chlorophyta)

A 36 Kilodalton Limiting-CO2 Induced Polypeptide of Chlamydomonas Is Distinct from the 37 Kilodalton Periplasmic Carbonic Anhydrase

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Effect of CO₂ Concentration on Protein Biosynthesis and Carbonic Anhydrase Expression in Chlamydomonas reinhardtii

A 36 Kilodalton Limiting-CO₂ Induced Polypeptide of Chlamydomonas Is Distinct from the 37 Kilodalton Periplasmic Carbonic Anhydrase