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Structure and Function of Cema Homologue (PXCA) in Cyanobacteria

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Book cover The Chloroplast: From Molecular Biology to Biotechnology

Part of the book series: NATO Science Series ((ASHT,volume 64))

Abstract

The cemA (ycf10) gene codes for a chloroplast envelope membrane protein [1] and is conserved in higher and lower plants and in algae [2–8]. CemA in higher plants consists of 229 to 231 amino-acids [2–4] whereas that in liverwort (Marchantia) [5] and Chlamydomonas [6] is much larger and consists of 434 and 500 amino-acids, respectively. Recent sequencing of whole chloroplast genomes of Porphyra [7] and Chlorella [8] revealed that cemA in these algae encodes proteins of 278 and 264 amino-acids, respectively. The function of CemA is not known. Rolland et al [6] have constructed mutants by disrupting cemA in Chlamydomonas. They showed that the disruption of the gene led to increased light sensitivity and affected CO2-dependent photosynthesis and inorganic carbon uptake.

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© 1999 Springer Science+Business Media Dordrecht

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Sonoda, M., Katoh, H., Katoh, A., Ohkawa, H., Vermaas, W., Ogawa, T. (1999). Structure and Function of Cema Homologue (PXCA) in Cyanobacteria. In: Argyroudi-Akoyunoglou, J.H., Senger, H. (eds) The Chloroplast: From Molecular Biology to Biotechnology. NATO Science Series, vol 64. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-4788-0_23

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  • DOI: https://doi.org/10.1007/978-94-011-4788-0_23

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-0-7923-5577-9

  • Online ISBN: 978-94-011-4788-0

  • eBook Packages: Springer Book Archive

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