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Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta)

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Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta). / van Hunnik, E; Livne, A; Pogenberg, V; Spijkerman, E; van den Ende, H; Mendoza, E G; Sültemeyer, D; de Leeuw, J W.

In: PLANTA, Vol. 212, No. 3, 02.2001, p. 454-9.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

van Hunnik, E, Livne, A, Pogenberg, V, Spijkerman, E, van den Ende, H, Mendoza, EG, Sültemeyer, D & de Leeuw, JW 2001, 'Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta)', PLANTA, vol. 212, no. 3, pp. 454-9.

APA

van Hunnik, E., Livne, A., Pogenberg, V., Spijkerman, E., van den Ende, H., Mendoza, E. G., Sültemeyer, D., & de Leeuw, J. W. (2001). Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta). PLANTA, 212(3), 454-9.

Vancouver

van Hunnik E, Livne A, Pogenberg V, Spijkerman E, van den Ende H, Mendoza EG et al. Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta). PLANTA. 2001 Feb;212(3):454-9.

Bibtex

@article{7227f24a2d5249a9ad449b7c5bf9d83d,
title = "Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta)",
abstract = "In order to broaden our understanding of the eukaryotic CO2-concentrating mechanism the occurrence and localization of a thylakoid-associated carbonic anhydrase (EC 4.2.1.1) were studied in the green algae Tetraedron minimum and Chlamydomonas noctigama. Both algae induce a CO2-concentrating mechanism when grown under limiting CO2 conditions. Using mass-spectrometric measurements of 18O exchange from doubly labelled CO2, the presence of a thylakoid-associated carbonic anhydrase was confirmed for both species. From purified thylakoid membranes, photosystem I (PSI), photosystem II (PSII) and the light-harvesting complex of the photosynthetic apparatus were isolated by mild detergent gel. The protein fractions were identified by 77 K fluorescence spectroscopy and immunological studies. A polypeptide was found to immunoreact with an antibody raised against thylakoid carbonic anhydrase (CAH3) from Chlamydomonas reinhardtii. It was found that this polypeptide was mainly associated with PSII, although a certain proportion was also connected to light harvesting complex II. This was confirmed by activity measurements of carbonic anhydrase in isolated bands extracted from the mild detergent gel. The thylakoid carbonic anhydrase isolated from T. minimum had an isoelectric point between 5.4 and 4.8. Together the results are consistent with the hypothesis that thylakoid carbonic anhydrase resides within the lumen where it is associated with the PSII complex.",
keywords = "Animals, Carbon Dioxide/chemistry, Carbonic Anhydrases/metabolism, Chlamydomonas/enzymology, Chlorophyta/enzymology, Electrophoresis, Polyacrylamide Gel, Immunoblotting, In Vitro Techniques, Mass Spectrometry, Photosynthetic Reaction Center Complex Proteins/analysis, Photosystem I Protein Complex, Photosystem II Protein Complex, Spectrometry, Fluorescence, Thylakoids/chemistry",
author = "{van Hunnik}, E and A Livne and V Pogenberg and E Spijkerman and {van den Ende}, H and Mendoza, {E G} and D S{\"u}ltemeyer and {de Leeuw}, {J W}",
year = "2001",
month = feb,
language = "English",
volume = "212",
pages = "454--9",
journal = "PLANTA",
issn = "0032-0935",
publisher = "Springer",
number = "3",

}

RIS

TY - JOUR

T1 - Identification and localization of a thylakoid-bound carbonic anhydrase from the green algae Tetraedron minimum (Chlorophyta) and Chlamydomonas noctigama (Chlorophyta)

AU - van Hunnik, E

AU - Livne, A

AU - Pogenberg, V

AU - Spijkerman, E

AU - van den Ende, H

AU - Mendoza, E G

AU - Sültemeyer, D

AU - de Leeuw, J W

PY - 2001/2

Y1 - 2001/2

N2 - In order to broaden our understanding of the eukaryotic CO2-concentrating mechanism the occurrence and localization of a thylakoid-associated carbonic anhydrase (EC 4.2.1.1) were studied in the green algae Tetraedron minimum and Chlamydomonas noctigama. Both algae induce a CO2-concentrating mechanism when grown under limiting CO2 conditions. Using mass-spectrometric measurements of 18O exchange from doubly labelled CO2, the presence of a thylakoid-associated carbonic anhydrase was confirmed for both species. From purified thylakoid membranes, photosystem I (PSI), photosystem II (PSII) and the light-harvesting complex of the photosynthetic apparatus were isolated by mild detergent gel. The protein fractions were identified by 77 K fluorescence spectroscopy and immunological studies. A polypeptide was found to immunoreact with an antibody raised against thylakoid carbonic anhydrase (CAH3) from Chlamydomonas reinhardtii. It was found that this polypeptide was mainly associated with PSII, although a certain proportion was also connected to light harvesting complex II. This was confirmed by activity measurements of carbonic anhydrase in isolated bands extracted from the mild detergent gel. The thylakoid carbonic anhydrase isolated from T. minimum had an isoelectric point between 5.4 and 4.8. Together the results are consistent with the hypothesis that thylakoid carbonic anhydrase resides within the lumen where it is associated with the PSII complex.

AB - In order to broaden our understanding of the eukaryotic CO2-concentrating mechanism the occurrence and localization of a thylakoid-associated carbonic anhydrase (EC 4.2.1.1) were studied in the green algae Tetraedron minimum and Chlamydomonas noctigama. Both algae induce a CO2-concentrating mechanism when grown under limiting CO2 conditions. Using mass-spectrometric measurements of 18O exchange from doubly labelled CO2, the presence of a thylakoid-associated carbonic anhydrase was confirmed for both species. From purified thylakoid membranes, photosystem I (PSI), photosystem II (PSII) and the light-harvesting complex of the photosynthetic apparatus were isolated by mild detergent gel. The protein fractions were identified by 77 K fluorescence spectroscopy and immunological studies. A polypeptide was found to immunoreact with an antibody raised against thylakoid carbonic anhydrase (CAH3) from Chlamydomonas reinhardtii. It was found that this polypeptide was mainly associated with PSII, although a certain proportion was also connected to light harvesting complex II. This was confirmed by activity measurements of carbonic anhydrase in isolated bands extracted from the mild detergent gel. The thylakoid carbonic anhydrase isolated from T. minimum had an isoelectric point between 5.4 and 4.8. Together the results are consistent with the hypothesis that thylakoid carbonic anhydrase resides within the lumen where it is associated with the PSII complex.

KW - Animals

KW - Carbon Dioxide/chemistry

KW - Carbonic Anhydrases/metabolism

KW - Chlamydomonas/enzymology

KW - Chlorophyta/enzymology

KW - Electrophoresis, Polyacrylamide Gel

KW - Immunoblotting

KW - In Vitro Techniques

KW - Mass Spectrometry

KW - Photosynthetic Reaction Center Complex Proteins/analysis

KW - Photosystem I Protein Complex

KW - Photosystem II Protein Complex

KW - Spectrometry, Fluorescence

KW - Thylakoids/chemistry

M3 - SCORING: Journal article

C2 - 11289611

VL - 212

SP - 454

EP - 459

JO - PLANTA

JF - PLANTA

SN - 0032-0935

IS - 3

ER -