mRNA export and gene expression: The SAGA–TREX-2 connection

García-Oliver, Encar; García-Molinero, Varinia; Rodrı́guez-Navarro, Susana

doi:10.1016/j.bbagrm.2011.11.011

Cited by 81 publications

(74 citation statements)

References 161 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…1A). Given that the histone acetylation and deubiquitylation activities of the SAGA complex are rendered by Gcn5 and Ubp8 (García-Oliver et al, 2012), these results suggest that SAGA complex regulates cell separation independent of its enzymatic activities.…”

Section: Resultsmentioning

confidence: 94%

See 1 more Smart Citation

Septin ring assembly is regulated by Spt20, a structural subunit of SAGA complex

Lei¹,

Zhou²,

Guo³

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

BSTRACTAccurate cell division requires the proper assembly of high-order septin structures. In fission yeast (Schizosaccharomyces pombe), Spn1-Spn4 are assembled into a primary septin ring at the division site, and the subsequent recruitment of Mid2 to the structure results in a stable septin ring. However, not much is known about the regulation of this key process. Here, we found that deletion of Spt20, a structural subunit of the Spt-Ada-Gcn5-acetyltransferase (SAGA) transcriptional activation complex, caused a severe cell separation defect. The defect was mainly due to impaired septin ring assembly, as 80% of spt20D cells lost septin rings at the division sites. Spt20 regulates septin ring assembly partially through the transcriptional activation of mid2 + . Spt20 also interacted with Spn2 and Mid2 in vitro and was associated with other components of the ring in vivo. Spt20 colocalized with the septin ring, but did not separate when the septin ring split. Importantly, Spt20 regulated the stability of the septin ring and was required for the recruitment of Mid2. The transcription-dependent and -independent roles of Spt20 in septin ring assembly highlight a multifaceted regulation of one process by a SAGA subunit.

show abstract

Section: Resultsmentioning

confidence: 94%

“…It is implicated in transcriptional initiation, elongation and mRNA export (García-Oliver et al, 2012). The SAGA complex can be organized into at least five modules with distinct activities.…”

Section: Introductionmentioning

confidence: 99%

Septin ring assembly is regulated by Spt20, a structural subunit of SAGA complex

Lei¹,

Zhou²,

Guo³

et al. 2014

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…Furthermore, the role of the SAGA complex and Thp1 in transcription elongation suggests that TREX-2, analogous to TREX, may define a pathway connecting transcription elongation with mRNA export. 90 The Drosophila homolog of Sus1, ENY2, is also co-transcriptionally recruited to nascent mRNAs, indicating the evolutionarily conserved role of Sus1/ENY2 in mRNA export. 95 However, the association of ENY2 with components of THO instead of TREX-2 suggests that Sus1/ENY2 may participate in mRNA export, in conjunction with similar but somewhat different complexes, in higher eukaryotic cells.…”

Section: Introductionmentioning

confidence: 99%

“…90 The TREX-2 complex consists of Sac3, Thp1, Cdc31 and the Spt-Ada-Gcn5 acetyltransferase (SAGA) complex. 91,92 Sac3 interacts with Mex67/Mtr2 and a component of the nuclear pore complex, Nup1, and facilitates docking of mRNPs to the nuclear pore.…”

Section: Introductionmentioning

confidence: 99%

Coupling pre-mRNA processing to transcription on the RNA factory assembly line

Lee

Tarn

2013

RNA Biology

View full text Add to dashboard Cite

“…Sus1 functions in histone deubiquitination and mRNA export are affected in I2 hairpin mutants that inhibit splicing Sus1 is a conserved factor that is required for mRNA export and histone H2B deubiquitination, and deletion or mutation of SUS1 has been shown to impair mRNA export and histone H2B deubiquitination (Rodríguez-Navarro et al 2004; Köhler et al 2006;Kurshakova et al 2007;Zhao et al 2008;Klöckner et al 2009;Kopytova et al 2010;Galan and Rodríguez-Navarro 2012;García-Oliver et al 2012). So far, our analyses have shown that partial deletion (I2-mut1) and stabilization (I2-mut3) of the 37-nt hairpin structure formed by intron 2 led to differential SUS1 isoform expression.…”

Section: Stabilization Of the Intron 2 Hairpin Affects Sus1 Expressionmentioning

confidence: 99%

An intronic RNA structure modulates expression of the mRNA biogenesis factor Sus1

AbuQattam

Gallego

Rodrı́guez-Navarro

2015

RNA

Self Cite

View full text Add to dashboard Cite

Sus1 is a conserved protein involved in chromatin remodeling and mRNA biogenesis. Unlike most yeast genes, the SUS1 premRNA of Saccharomyces cerevisiae contains two introns and is alternatively spliced, retaining one or both introns in response to changes in environmental conditions. SUS1 splicing may allow the cell to control Sus1 expression, but the mechanisms that regulate this process remain unknown. Using in silico analyses together with NMR spectroscopy, gel electrophoresis, and UV thermal denaturation experiments, we show that the downstream intron (I2) of SUS1 forms a weakly stable, 37-nucleotide stem-loop structure containing the branch site near its apical loop and the 3 ′ splice site after the stem terminus. A cellular assay revealed that two of four mutants containing altered I2 structures had significantly impaired SUS1 expression. Semiquantitative RT-PCR experiments indicated that all mutants accumulated unspliced SUS1 pre-mRNA and/or induced distorted levels of fully spliced mRNA relative to wild type. Concomitantly, Sus1 cellular functions in histone H2B deubiquitination and mRNA export were affected in I2 hairpin mutants that inhibited splicing. This work demonstrates that I2 structure is relevant for SUS1 expression, and that this effect is likely exerted through modulation of splicing.

show abstract

mRNA export and gene expression: The SAGA–TREX-2 connection

Cited by 81 publications

References 161 publications

Septin ring assembly is regulated by Spt20, a structural subunit of SAGA complex

Septin ring assembly is regulated by Spt20, a structural subunit of SAGA complex

Coupling pre-mRNA processing to transcription on the RNA factory assembly line

An intronic RNA structure modulates expression of the mRNA biogenesis factor Sus1

Contact Info

Product

Resources

About