Os01g0267900

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Annotated Information

Function

OsCam1-1; OsCam1-2 and OsCam1-3 encode identical proteins, whereas OsCam2 and OsCam3 encode a protein of only two amino acid differences and their sequences share 98.7% identity with those of OsCaM1 proteins.OsCam1-1, OsCam1-2, and OsCam1-3 genes encode identical proteins.

Expression

Bands of the expected sizes based on each of the gene sequences (698, 526, 551, 201, and 520 base pairs for OsCam1-2, OsCam1-2, OsCam1-3, OsCam2, and OsCam3, respectively) were detected in all organs or tissues examined including the leaves and roots of 2-week old seedlings, mature leaves, flowers, immature seeds and calli. No band was detected in the control RTPCR reactions. It should be noted that the RT-PCR conditions used in this study did not allow quantitative deter mination, therefore comparison of the expression levels among different organs or different genes can not be made. Nevertheless, it can be concluded that all of OsCam genes were expressed in all organs that we examined.

Evolution

Interestingly, all of the intron-containing OsCML genes are also interrupted by an intron at the same location as OsCam genes. The conservation of this intron position indicates their close relationships which is consistent with the fact that these genes encode members of the CML proteins groups 1-4, closely-related CaM-like proteins to OsCaMs. OsCML1, OsCML2, and OsCML3 genes contain an additional intron that resides at the codon corresponding to the last residue of genes encoding conventional CaMs. These proteins have an extended C-terminal basic domain and a putative prenylation site. The position of these introns reflects the separation of functional domains within these proteins and suggests that the sequences encoding their carboxyl extensions arose later in the evolution by the fusion of existing Cam genes to the additional exons.

Labs working on this gene

Department of Biochemistry, Faculty of Science, Chulalongkorn University, Payathai Road, Patumwan, Bangkok 10330, Thailand

References

1. Bongkoj Boonburapong;Teerapong Buaboocha

 Genome-wide identification and analyses of the rice calmodulin and related potential calcium sensor proteins
 BMC Plant Biology, 2007, 7: 4