Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing

Li, Hao; Bingham, Paul M.

doi:10.1016/0092-8674(91)90185-2

Cited by 211 publications

(156 citation statements)

References 26 publications

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“…In most cases, the principles and mechanisms of subnuclear topogenesis are not clear. Only the binding of some proteins to nucleic acids, be it sequence-specific or broadly selective, has been studied to some extent (Bandziulis et al, 1989;Van Holde, 1989;Churchill and Travers, 1991;Li and Bingham, 1991;Tafuri and Wolffe, 1993). Moreover, sequence requirements for the assembly of karyoskeletal proteins of the lamin group into a lamina associated with the inner nuclear membrane have been determined (Loewinger and McKeon, 1988;Holtz et al, 1989;Krohne et al, 1989;Kitten and Nigg, 1991;Smith and Blobel, 1993;Soullam and Worman, 1993;Meier and Georgatos, 1994).…”

Section: Introductionmentioning

confidence: 99%

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

Zirwes

Kouzmenko

Peters

et al. 1997

MBoC

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To identify the element(s) in nucleolar proteins which determine nucleolus-specific topogenesis, we have used different kinds of cDNA constructs encoding various chimeric combinations of mutants of the constitutive nucleolar protein N038 (B23): 1) with an amino terminally placed short "myc tag"; 2) with two different carboxyl terminally attached large a-helical coiled coil structures, the lamin A rod domain or the rod domain of vimentin; 3) with the sequence-related nucleoplasmic histone-binding protein nucleoplasmin; and 4) with the soluble cytoplasmic protein pyruvate kinase. To avoid the problem of formation of complexes with endogenous wild-type (wt) molecules and "piggyback" localization, special care was taken to secure that the mutants and chimeras used did not oligomerize as is typical of protein N038 (B23). Using microinjection and transfection of cultured cells, we found that the segment comprising the amino-terminal 123 amino acids (aa) alone was sufficient to effect nucleolar accumulation of the construct molecules, including the chimeras with the entire rod domains of lamin A and vimentin. However, when the amino-terminal 109 aa were deleted, the molecules still associated with the nucleolus. The results of further deletion experiments and of domain swaps with nucleoplasmin all point to the topogenic importance of two independent molecular regions located at both the amino-and carboxyl-terminal end. Our definition of dominant elements determining the nucleolar localization of protein N038 (B23) as well as of diverse nonnucleolar proteins will help to identify its local binding partner(s) and functions, the construction of probes examining other proteins or sequence elements within the nucleolar microenvironment, and the generation of cells with an altered nuclear architecture.

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Section: Introductionmentioning

confidence: 99%

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

Zirwes

Kouzmenko

Peters

et al. 1997

MBoC

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“…The three PGC-1 homologues share an aminoterminal activation domain with LXXLL signature motifs involved in nuclear receptor docking [6] and interaction with other transcriptional coactivators such as the steroid receptor coactivator-1 (SRC-1)/p300 complex [9], a nuclear localisation signal (NLS), and a C-terminal RNA recognition motif (RRM) [1]. PGC-1α and PRC share an additional carboxy-terminal sequence, the arginine-serine-rich (RS) domain [1], that is characteristic of proteins involved in mRNA processing and splicing [10]. The C-terminal region of PGC-1α1 has been shown to be essential for interaction with the Mediator complex, and thus the transcriptional machinery, via Mediator of RNA polymerase II transcription subunit 1 (MED1) [9].…”

Section: Introductionmentioning

confidence: 99%

The hitchhiker’s guide to PGC-1α isoform structure and biological functions

2015

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Proteins of the peroxisome proliferator-activated receptor γ (PPARγ) coactivator 1 (PGC-1) family of transcriptional coactivators coordinate physiological adaptations in many tissues, usually in response to demands for higher nutrient and energy supply. Of the founding members of the family, PGC-1α (also known as PPARGC1A) is the most highly regulated gene, using multiple promoters and alternative splicing to produce a growing number of coactivator variants. PGC-1α promoters are selectively active in distinct tissues in response to specific stimuli. To date, more than ten novel PGC-1α isoforms have been reported to be expressed from a novel promoter (PGC-1α-b, PGC-1α-c), to undergo alternative splicing (NT-PGC-1α) or both (PGC-1α2, PGC-1α3, PGC-1α4). The resulting proteins display differential regulation and tissue distribution and, most importantly, exert specific biological functions. In this review we discuss the structural and functional characteristics of the novel PGC-1α isoforms, aiming to provide an integrative view of this constantly expanding system of transcriptional coactivators.

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“…The RNA-binding specificity of an SR protein is conferred by the RRM region and adjacent sequences (Cá ceres and Krainer 1993;Zuo and Manley 1993;Tacke and Manley 1995;Allain and Howe 1997;Tacke et al 1997); the various RS domains are responsible primarily for proteinprotein interactions, which are modulated by the phosphorylation status of these regions (Wu and Maniatis 1993;Amrein et al 1994;Kohtz et al 1994;Zuo and Maniatis 1996;Xiao and Manley 1997). In addition, it has been demonstrated that RS domains modulate the RNAbinding activity and subnuclear localization of SR proteins (Li and Bingham 1991;Hedley et al 1995;Cá ceres et al 1997). Recently, SF2/ASF, SRp20, and 9G8 have been shown to shuttle between the nucleus and the cytoplasm, and this property depends on the presence and type of RS domain (Cá ceres et al 1998).…”

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confidence: 99%

atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana, regulates splicing of specific plant genes

Lopato¹,

Kalyna²,

Dorner³

et al. 1999

Genes & Development

150

199

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SR proteins are nuclear phosphoproteins with a characteristic Ser/Arg-rich domain and one or two RNA recognition motifs. They are highly conserved in animals and plants and play important roles in spliceosome assembly and alternative splicing regulation. We have now isolated and partially sequenced a plant protein, which crossreacts with antibodies to human SR proteins. The sequence of the corresponding cDNA and genomic clones from Arabidopsis revealed a protein, atSRp30, with strong similarity to the human SR protein SF2/ASF and to atSRp34/SR1, a previously identified SR protein, indicating that plants possess two SF2/ASF-like proteins. atSRp30 expresses alternatively spliced mRNA isoforms that are expressed differentially in various organs and during development. Overexpression of atSRp30 via a strong constitutive promoter resulted in changes in alternative splicing of several endogenous plant genes, including atSRp30 itself. Interestingly, atSRp30 overexpression resulted in a pronounced down-regulation of endogenous mRNA encoding full-length atSRp34/SR1 protein. Transgenic plants overexpressing atSRp30 showed morphological and developmental changes affecting mostly developmental phase transitions. atSRp30-and atSRp34/ SR1-promoter-GUS constructs exhibited complementary expression patterns during early seedling development and root formation, with overlapping expression in floral tissues. The results of the structural and expression analyses of both genes suggest that atSRp34/SR1 acts as a general splicing factor, whereas atSRp30 functions as a specific splicing modulator.

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Arginine/serine-rich domains of the su(wa) and tra RNA processing regulators target proteins to a subnuclear compartment implicated in splicing

Cited by 211 publications

References 26 publications

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

Topogenesis of a nucleolar protein: determination of molecular segments directing nucleolar association.

The hitchhiker’s guide to PGC-1α isoform structure and biological functions

atSRp30, one of two SF2/ASF-like proteins from Arabidopsis thaliana, regulates splicing of specific plant genes

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