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Isolation and Expression Analysis of Three Types of α-Carbonic Anhydrases from the Antarctic Alga Chlamydomonas sp. ICE-L under Different Light Stress Treatments.
- Source :
-
Molecular biotechnology [Mol Biotechnol] 2019 Mar; Vol. 61 (3), pp. 200-208. - Publication Year :
- 2019
-
Abstract
- Carbonic anhydrases (CAs) are a class of zinc-containing metalloenzymes that can reversibly catalyse the hydration reaction of carbon dioxide. Antarctic algae are the most critical component of the Antarctic ecosystem; algae can enter the carbon cycle food chain by fixing carbon dioxide from the air. In this study, the complete open reading frames (ORFs) of CA1 (GenBank ID KY826431), CA2 (GenBank ID KY826432), and CA3 (GenBank ID KY826433), encoding CAs in the Antarctic ice microalga Chlamydomonas. sp. ICE-L, were successfully cloned using reverse transcription-polymerase chain reaction (RT-PCR). In addition, the expression patterns of CAs under blue light, under UV light, and in the dark were determined by quantitative reverse transcription-polymerase chain reaction (qRT-PCR). The CA1, CA2, and CA3 ORFs encode proteins of 376, 430, and 419 amino acids, respectively. Phylogenetic analysis revealed that all amino acid sequences showed high homology with those of C. sp. ICE-L. There are six types of algal CAs; we hypothesised that the CAs studied here are most likely α-CAs. Expression analysis showed that the transcription level of the CAs was influenced by both UV light and blue light. These findings provide additional insight into the molecular mechanisms of CAs and will accelerate the development of CAs for applications in agriculture and environmental governance.
- Subjects :
- Algal Proteins chemistry
Algal Proteins genetics
Algal Proteins metabolism
Amino Acid Sequence
Base Sequence
Carbonic Anhydrases chemistry
Chlamydomonas genetics
Evolution, Molecular
Models, Molecular
Open Reading Frames
Phylogeny
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Carbonic Anhydrases genetics
Carbonic Anhydrases metabolism
Chlamydomonas enzymology
Cloning, Molecular drug effects
Subjects
Details
- Language :
- English
- ISSN :
- 1559-0305
- Volume :
- 61
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Molecular biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 30649663
- Full Text :
- https://doi.org/10.1007/s12033-018-00152-4