Novel alternative splicing of mRNAs encoding poly(A) polymerases in Arabidopsis

Addepalli, Balasubrahmanyam; Meeks, Lisa R.; Forbes, Kevin P.; Hunt, Arthur G.

doi:10.1016/j.bbaexp.2004.06.001

Cited by 22 publications

(33 citation statements)

References 36 publications

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“…1A) was amplified from cDNA using primers Nter and F (Table I); primer F is unique to the smaller of the two At1g30460 transcripts and thus does not amplify the coding region for the N terminus of the AtCPSF30-YT521-B polypeptide. PCR products were cloned into pGEM and the inserts sequenced as described (Addepalli et al, 2004). The AtCPSF30 fragment was excised with BglII and cloned into BamHIdigested pMALC2 (New England Biolabs).…”

Section: Production Of Atcpsf30 In Escherichia Colimentioning

confidence: 99%

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Calmodulin Interacts with and Regulates the RNA-Binding Activity of an Arabidopsis Polyadenylation Factor Subunit

et al. 2006

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The Arabidopsis (Arabidopsis thaliana) gene that encodes the probable ortholog of the 30-kD subunit of the mammalian cleavage and polyadenylation specificity factor (CPSF) is a complex one, encoding small (approximately 28 kD) and large (approximately 68 kD) polypeptides. The small polypeptide (AtCPSF30) corresponds to CPSF30 and is the focus of this study. Recombinant AtCPSF30 was purified from Escherichia coli and found to possess RNA-binding activity. Mutational analysis indicated that an evolutionarily conserved central core of AtCPSF30 is involved in RNA binding, but that RNA binding also requires a short sequence adjacent to the N terminus of the central core. AtCPSF30 was found to bind calmodulin, and calmodulin inhibited the RNA-binding activity of the protein in a calcium-dependent manner. Mutational analysis showed that a small part of the protein, again adjacent to the N terminus of the conserved core, is responsible for calmodulin binding; point mutations in this region abolished both binding to and inhibition of RNA binding by calmodulin. Interestingly, AtCPSF30 was capable of self-interactions. This property also mapped to the central conserved core of the protein. However, calmodulin had no discernible effect on the self-association. These results show that the central portion of AtCPSF30 is involved in a number of important functions, and they raise interesting possibilities for both the interplay between splicing and polyadenylation and the regulation of these processes by stimuli that act through calmodulin.

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Section: Production Of Atcpsf30 In Escherichia Colimentioning

confidence: 99%

“…DNAs encoding the AtCPSF30 coding region were isolated from total RNA by RT-PCR as described elsewhere (Addepalli et al, 2004). The coding region for the smaller At1g30460-encoded protein (Fig.…”

Section: Production Of Atcpsf30 In Escherichia Colimentioning

confidence: 99%

Calmodulin Interacts with and Regulates the RNA-Binding Activity of an Arabidopsis Polyadenylation Factor Subunit

et al. 2006

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“…PAPS3 resembles PAPOLB in lacking an extended C-terminal region, being localized in the cytoplasm and expressed mainly in the male gametophytes (the pollen). By contrast, PAPS1, PAPS2, and PAPS4 all contain an extended C-terminal region, localize exclusively to the nucleus, and are expressed throughout the plant (2,(16)(17)(18). All four proteins have nonspecific polyadenylation activity in vitro, suggesting that they represent functional cPAPSs (16,19).…”

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confidence: 99%

“…By contrast, PAPS1, PAPS2, and PAPS4 all contain an extended C-terminal region, localize exclusively to the nucleus, and are expressed throughout the plant (2,(16)(17)(18). All four proteins have nonspecific polyadenylation activity in vitro, suggesting that they represent functional cPAPSs (16,19). On the basis of the failure to identify homozygous transfer DNA (T-DNA) insertion mutants for any of the three genes, it was concluded that all of them are essential for plant growth and development (17).…”

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Target specificity among canonical nuclear poly(A) polymerases in plants modulates organ growth and pathogen response

Lang

Trost

Lange

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Polyadenylation of pre-mRNAs is critical for efficient nuclear export, stability, and translation of the mature mRNAs, and thus for gene expression. The bulk of pre-mRNAs are processed by canonical nuclear poly(A) polymerase (PAPS). Both vertebrate and higher-plant genomes encode more than one isoform of this enzyme, and these are coexpressed in different tissues. However, in neither case is it known whether the isoforms fulfill different functions or polyadenylate distinct subsets of pre-mRNAs. Here we show that the three canonical nuclear PAPS isoforms in Arabidopsis are functionally specialized owing to their evolutionarily divergent C-terminal domains. A strong loss-of-function mutation in PAPS1 causes a male gametophytic defect, whereas a weak allele leads to reduced leaf growth that results in part from a constitutive pathogen response. By contrast, plants lacking both PAPS2 and PAPS4 function are viable with wild-type leaf growth. Polyadenylation of SMALL AUXIN UP RNA (SAUR) mRNAs depends specifically on PAPS1 function. The resulting reduction in SAUR activity in paps1 mutants contributes to their reduced leaf growth, providing a causal link between polyadenylation of specific pre-mRNAs by a particular PAPS isoform and plant growth. This suggests the existence of an additional layer of regulation in plant and possibly vertebrate gene expression, whereby the relative activities of canonical nuclear PAPS isoforms control de novo synthesized poly(A) tail length and hence expression of specific subsets of mRNAs.

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Regulation of Gene Expression in Plants

Bassett¹

2007

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Novel alternative splicing of mRNAs encoding poly(A) polymerases in Arabidopsis

Cited by 22 publications

References 36 publications

Calmodulin Interacts with and Regulates the RNA-Binding Activity of an Arabidopsis Polyadenylation Factor Subunit

Calmodulin Interacts with and Regulates the RNA-Binding Activity of an Arabidopsis Polyadenylation Factor Subunit

Target specificity among canonical nuclear poly(A) polymerases in plants modulates organ growth and pathogen response

Regulation of Gene Expression in Plants

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