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Cloning and characterization of the Rubisco activase gene from Ipomoea batatas (L.) Lam

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Abstract

A full-length cDNA of Rubisco activase (IBrcaI) was cloned from sweet potato (Ipomoea batatas (L.) Lam) using Rapid-Amplification of cDNA Ends (RACE). IBrcaI contains a 1,347 bp open reading frame encoding a protein of 439 amino acids. The sequence alignment of multiple Rubisco activase genes from sweet potato and other plants showed high homology at two previously described ATP-binding sites. Western blot analysis indicated that there are two Rubisco activase proteins in sweet potato. Expression of IBrcaI was only detected in leaves. In the 14 h light and 10 h dark photoperiods, maximal and minimal IBrcaI mRNA expression levels were detected at 8:00 in the morning and at midnight, respectively.

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  1. Sichuan Key Laboratory of Molecular Biology and Biotechnology, College of Life Science, Sichuan University, 610064, Chengdu, People’s Republic of China

    Ke Xu, Bowen He, Shuang Zhou, Yi Li & Yizheng Zhang

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  1. Ke Xu
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  2. Bowen He
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  3. Shuang Zhou
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Correspondence to Yizheng Zhang.

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Xu, K., He, B., Zhou, S. et al. Cloning and characterization of the Rubisco activase gene from Ipomoea batatas (L.) Lam. Mol Biol Rep 37, 661–668 (2010). https://doi.org/10.1007/s11033-009-9510-x

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  • DOI: https://doi.org/10.1007/s11033-009-9510-x

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