Identification of a new chloroplast carbonic anhydrase in Chlamydomonas reinhardtii
Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCM...
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| Published in: | Plant physiology (Bethesda) Vol. 135; no. 1; pp. 173 - 182 |
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| Main Authors: | , , , , |
| Format: | Journal Article |
| Language: | English |
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Rockville, MD
American Society of Plant Biologists
01.05.2004
American Society of Plant Physiologists |
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| ISSN: | 0032-0889, 1532-2548 |
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| Abstract | Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Her e we identify a sixth gene encoding a beta-type CA. This new beta-CA, designated Cah6, is d istinct from the two mitochondrial beta-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. |
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| AbstractList | Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Her e we identify a sixth gene encoding a beta-type CA. This new beta-CA, designated Cah6, is d istinct from the two mitochondrial beta-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated α-, β-, and γ-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Here we identify a sixth gene encoding a β-type CA. This new β-CA, designated Cah6, is distinct from the two mitochondrial β-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Here we identify a sixth gene encoding a beta-type CA. This new beta-CA, designated Cah6, is distinct from the two mitochondrial beta-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO sub(2). The three evolutionarily unrelated families of CAs are designated alpha -, beta -, and gamma -CA. Aquatic photosynthetic organisms have evolved different forms of CO sub(2) concentrating mechanisms (CCMs) to aid Rubisco in capturing CO sub(2) from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Here we identify a sixth gene encoding a beta -type CA. This new beta -CA, designated Cah6, is distinct from the two mitochondrial beta -CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Here we identify a sixth gene encoding a beta-type CA. This new beta-CA, designated Cah6, is distinct from the two mitochondrial beta-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed.Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs are designated alpha-, beta-, and gamma-CA. Aquatic photosynthetic organisms have evolved different forms of CO2 concentrating mechanisms (CCMs) to aid Rubisco in capturing CO2 from the surrounding environment. One aspect of all CCMs is the critical roles played by various specially localized extracellular and intracellular CAs. Five CAs have previously been identified in Chlamydomonas reinhardtii, a green alga with a well-studied CCM. Here we identify a sixth gene encoding a beta-type CA. This new beta-CA, designated Cah6, is distinct from the two mitochondrial beta-CAs in C. reinhardtii. Nucleotide sequence data show that the Cah6 cDNA contains an open reading frame encoding a polypeptide of 264 amino acids with a leader sequence likely targeting the protein to the chloroplast stroma. We have fused the Cah6 open reading frame to the coding sequence of maltose-binding protein in a pMal expression vector. The purified recombinant fusion protein is active and was used to partially characterize the Cah6 protein. The purified recombinant fusion protein was cleaved with protease Factor Xa to separate Cah6 from the maltose-binding protein and the purified Cah6 protein was used to raise an antibody. Western blots, immunolocalization studies, and northern blots collectively indicated that Cah6 is constitutively expressed in the stroma of chloroplasts. A possible role for Cah6 in the CCM of C. reinhardtii is proposed. |
| Author | Ynalvez, R.A Mitra, M Lato, S.M Xiao, Y Moroney, J.V |
| AuthorAffiliation | Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803 |
| AuthorAffiliation_xml | – name: Department of Biological Sciences, Louisiana State University, Baton Rouge, Louisiana 70803 |
| Author_xml | – sequence: 1 fullname: Mitra, M – sequence: 2 fullname: Lato, S.M – sequence: 3 fullname: Ynalvez, R.A – sequence: 4 fullname: Xiao, Y – sequence: 5 fullname: Moroney, J.V |
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| Keywords | Nucleotide sequence Enzyme Algae Carbon dioxide Ribulose-bisphosphate carboxylase Lyases Chlorophyceae Peptidases Binding protein Carbon-carbon lyases Chlorophyta Complementary DNA Gene Carboxy-lyases Aminoacid Chlamydomonas reinhardtii Hydrolases Carbonate dehydratase Photosynthesis Carbon-oxygen lyases Chloroplast Hydro-lyases Thallophyta |
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| Notes | http://www.plantphysiol.org/ ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.037283. Corresponding author; e-mail btmoro@lsu.edu; fax 1–225–578–2597. Supported by National Science Foundation (grants IBN–9904425 and IBN–0212093 to J.V.M.) and the Howard Hughes Memorial Institute undergraduate research program. |
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| Snippet | Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO2. The three evolutionarily unrelated families of CAs... Carbonic anhydrases (CA) are zinc-containing metalloenzymes that catalyze the reversible hydration of CO sub(2). The three evolutionarily unrelated families of... |
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| SubjectTerms | Acclimatization algae algae and seaweeds Amino Acid Sequence amino acid sequences Animals Antibodies Bioenergetics and Photosynthesis Biological and medical sciences Blotting, Northern Blotting, Western Carbon Dioxide Carbon Dioxide - metabolism carbonate dehydratase Carbonic Anhydrases Carbonic Anhydrases - genetics Carbonic Anhydrases - metabolism chemistry Chlamydomonas reinhardtii Chlamydomonas reinhardtii - enzymology Chlamydomonas reinhardtii - genetics Chlamydomonas reinhardtii - ultrastructure Chlorophyta Chloroplasts Chloroplasts - enzymology Chloroplasts - ultrastructure Cloning, Molecular Complementary DNA Cosmids DNA libraries DNA, Complementary DNA, Complementary - chemistry DNA, Complementary - genetics DNA, Protozoan DNA, Protozoan - chemistry DNA, Protozoan - genetics enzyme activity Enzymes enzymology Freshwater Fundamental and applied biological sciences. Psychology Gels gene expression regulation Gene Expression Regulation, Enzymologic gene overexpression genetic vectors genetics Genome, Protozoan genomics Immunohistochemistry maltose-binding protein Metabolism Microscopy, Immunoelectron Models, Biological Molecular Sequence Data Northern blotting nucleotide sequences Photosynthesis, respiration. Anabolism, catabolism Plant cells Plant physiology and development Plant Proteins Plants Polymerase chain reaction purification recombinant fusion proteins Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism sequence alignment sequence analysis Sequence Analysis, DNA Sequence Homology, Amino Acid ultrastructure Western blotting |
| Title | Identification of a new chloroplast carbonic anhydrase in Chlamydomonas reinhardtii |
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