Single base substitution in OsCDC48 is responsible for premature senescence and death phenotype in rice

Abstract

A premature senescence and death 128 (psd128) mutant was isolated from an ethyl methane sulfonate‐induced rice IR64 mutant bank. The premature senescence phenotype appeared at the six‐leaf stage and the plant died at the early heading stage. psd128 exhibited impaired chloroplast development with significantly reduced photosynthetic ability, chlorophyll and carotenoid contents, root vigor, soluble protein content and increased malonaldehyde content. Furthermore, the expression of senescence‐related genes was significantly altered in psd128. The mutant trait was controlled by a single recessive nuclear gene. Using map‐based strategy, the mutation Oryza sativa cell division cycle 48 (OsCDC48) was isolated and predicted to encode a putative AAA‐type ATPase with 809 amino‐acid residuals. A single base substitution at position C2347T in psd128 resulted in a premature stop codon. Functional complementation could rescue the mutant phenotype. In addition, RNA interference resulted in the premature senescence and death phenotype. OsCDC48 was expressed constitutively in the root, stem, leaf and panicle. Subcellular analysis indicated that OsCDC48:YFP fusion proteins were located both in the cytoplasm and nucleus. OsCDC48 was highly conserved with more than 90% identity in the protein levels among plant species. Our results indicated that the impaired function of OsCDC48 was responsible for the premature senescence and death phenotype.

The major‐effect quantitative trait locus CsARN6.1 encodes an AAA ATPase domain‐containing protein that is associated with waterlogging stress tolerance by promoting adventitious root formation

“…Indeed, our previous proteomics and transcriptomic studies in Zaoer‐N and Pepino revealed that while the two lines exhibited a similar enzyme cascade as found in other plants in response to the waterlogging stress, Zaoer‐N was more efficient at regenerating ATP and NAD + and continuation of the glycolysis pathway to deal with the energy crisis from waterlogging (Xu et al ., , ). Typically, the AAA domain in the AAA ATPase has the conserved function of binding ATP and converting the energy from ATP hydrolysis into a force that promotes cell division, expansion, growth and development (Hicks‐Berger et al ., ; Huang et al ., ). In the present study, several experiments established linkage of ATPase activity to ARN6.1 candidate gene expression as well as AR formation in the waterlogging‐tolerant line Zaoer‐N.…”

RLS3, a protein with AAA+ domain localized in chloroplast, sustains leaf longevity in rice

“…The evidence shows that Clp proteins are key factors in regulating protein quality in chloroplasts. Recently, the identification of OsCDC48 , which encodes a putative AAA‐ATPase that confers premature senescence and the death phenotype in rice, was reported (Huang et al ). In this study, a single‐nucleotide transition at the splice site of the 10 th intron/11 th exon led to the premature stop codon in the AAA+ domain of the rls3 mutant, resulting in the functional defect of the RLS3 gene.…”

Rice OsAAA-ATPase1 is Induced during Blast Infection in a Salicylic Acid-Dependent Manner, and Promotes Blast Fungus Resistance

“…To assess how OsAAA-ATPase1-6 are related within the AAA-ATPase gene family, we performed a phylogenic comparison of the proteins predicted to be encoded by OsAAA-ATPase1-6 and several known rice AAA-ATPase proteins, including LMR/LRD6-6 [21,22], OsCDC48 [27], RuvBL1a [28], RLS3 [29], OsSKD1 [30], OsFtsH5 [31], and RFC5 [32], together with NtAAA1 [18,19] and AtOM66 [20]. OsAAA-ATPase1 was grouped within a subclade of proteins related to plant defense, including OsAAA-ATPase2-6, NtAAA1, and AtOM66, but, unexpectedly, distally with LMR/LRD6-6 ( Figure 1b).…”