Cloning and Characterization of an RNase-Related Protein Gene Preferentially Expressed in Rice Stems

Wei, June; Li, Anming; Li, Yin; Wang, Jing; Liu, Xiaobin; Liangshi, Liu; Xu, Zeng-Fu

doi:10.1271/bbb.70.1041

Cited by 10 publications

(8 citation statements)

References 32 publications

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“…As a consequence, these two proteins have clearly lost their ribonuclease activity, as previously described for RNase DIS (Salekdeh et al 2002) (a.k.a. OsRPP: Wei et al 2006), which corresponds to OsRNS4.…”

Section: Resultsmentioning

confidence: 99%

“…The most highly induced protein in that experiment, RNase DIS, has homology to RNase T2, but lacks the conserved residues in the active site of the enzyme. The same gene, although renamed OsRRP (Wei et al 2006), was reported to be expressed preferentially in stems and to be down-regulated in an increased tillering dwarf mutant. The biological role of this non-functional RNase is unknown (Wei et al 2006).…”

Section: Introductionmentioning

confidence: 99%

“…The same gene, although renamed OsRRP (Wei et al 2006), was reported to be expressed preferentially in stems and to be down-regulated in an increased tillering dwarf mutant. The biological role of this non-functional RNase is unknown (Wei et al 2006). Similar non-functional S-like RNase genes have been found in wheat (Chang et al 2003) and barley (Gausing 2000).…”

Section: Introductionmentioning

confidence: 99%

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RNase T2 genes from rice and the evolution of secretory ribonucleases in plants

et al. 2010

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The plant RNase T2 family is divided into two different subfamilies. S-RNases are involved in rejection of self-pollen during the establishment of self-incompatibility in three plant families. S-like RNases, on the other hand, are not involved in self-incompatibility, and although gene expression studies point to a role in plant defense and phosphate recycling, their biological roles are less well understood. Although S-RNases have been subjects of many phylogenetic studies, few have included an extensive analysis of S-like RNases, and genome-wide analyses to determine the number of S-like RNases in fully sequenced plant genomes are missing. We characterized the eight RNase T2 genes present in the Oryza sativa genome; and we also identified the full complement of RNase T2 genes present in other fully sequenced plant genomes. Phylogenetics and gene expression analyses identified two classes among the S-like RNase subfamily. Class I genes show tissue specificity and stress regulation. Inactivation of RNase activity has occurred repeatedly throughout evolution. On the other hand, Class II seems to have conserved more ancestral characteristics; and, unlike other S-like RNases, genes in this class are conserved in all plant species analyzed and most are constitutively expressed. Our results suggest that gene duplication resulted in high diversification of Class I genes. Many of these genes are differentially expressed in response to stress, and we propose that protein characteristics, such as the increase in basic residues can have a defense role independent of RNase activity. On the other hand, constitutive expression and phylogenetic conservation suggest that Class II S-like RNases may have a housekeeping role.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RNase T2 genes from rice and the evolution of secretory ribonucleases in plants

et al. 2010

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“…Catalytically active histidine residue (CAS II) is known to be essential to ribonucleic activity of T2-type RNases (Jost et al 1991;Taylor et al 1993;Irie 1999). We identified and kept the proteins that were apparently missing this residue, as well as proteins established as catalytically inactive in functional studies (MacIntosh et al 2010;Ohkama-Ohtsu et al 2004;Wei et al 2006;Gausing 2000;Van Damme et al 2000;Kim et al 2004).…”

Section: T2/s-rnase Sequences and Alignmentmentioning

confidence: 99%

“…We identified a set of 91 sequences either corresponding to proteins established to be catalytically inactive in functional studies (MacIntosh et al 2010;Ohkama-Ohtsu et al 2004;Wei et al 2006;Gausing 2000;Van Damme et al 2000;Kim et al 2004), or lacking a conserved histidine residue that is essential for ribonuclease activity (Jost et al 1991;Taylor et al 1993;Irie 1999).…”

Section: Phylogenetic Relationships Among T2/s-rnasesmentioning

confidence: 99%

The evolutionary history of plant T2/S-type ribonucleases

Ramanauskas

Igić

2017

Preprint

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A growing number of T2/S-RNases are being discovered in plant genomes. Members of this protein family have a variety of known functions, but the vast majority are still uncharacterized. We present data and analyses of phylogenetic relationships among T2/S-RNases, and pay special attention to the group that contains the female component of the most widespread system of self-incompatibility in flowering plants. The returned emphasis on the initially identified component of this mechanism yields important conjectures about its evolutionary context. First, we find that the clade involved in self-rejection (class III) is found exclusively in core eudicots, while the remaining clades contain members from other vascular plants. Second, certain features, such as intron patterns, isoelectric point, and conserved amino acid regions, help differentiate S-RNases, which are necessary for expression of self-incompatibility, from other T2/S-RNase family members. Third, we devise and present a set of approaches to clarify new S-RNase candidates from existing genome assemblies. We use genomic features to identify putative functional and relictual S-loci in genomes of plants with unknown mechanisms of self-incompatibility. The widespread occurrence of possible relicts suggests that the loss of functional self-incompatibility may leave traces long after the fact, and that this manner of molecular fossil-like data could be an important source of information about the history and distribution of both RNase-based and other mechanisms of self-incompatibility. Finally, we release a public resource intended to aid the search for S-locus RNases, and help provide increasingly detailed information about their taxonomic distribution.

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RNase T2 Family: Enzymatic Properties, Functional Diversity, and Evolution of Ancient Ribonucleases

MacIntosh¹

2011

Nucleic Acids and Molecular Biology

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Cloning and Characterization of an RNase-Related Protein Gene Preferentially Expressed in Rice Stems

Cited by 10 publications

References 32 publications

RNase T2 genes from rice and the evolution of secretory ribonucleases in plants

RNase T2 genes from rice and the evolution of secretory ribonucleases in plants

The evolutionary history of plant T2/S-type ribonucleases

RNase T2 Family: Enzymatic Properties, Functional Diversity, and Evolution of Ancient Ribonucleases

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