Architectural features of pre‐mRNA introns in the fission yeast <i>Schizosaccharmyces pombe</i>

Prabhala, Ganesh; Rosenberg, George H.; Käufer, Norbert F.

doi:10.1002/yea.320080303

Cited by 87 publications

(62 citation statements)

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“…The results support the view that phosphorylation of SR-related proteins may serve as a mechanism for pre-mRNA splicing regulation in S. pombe, particularly considering that S. pombe has many introns with degenerate consensus sequences [22,[46][47][48] and the polypyrimidine tract downstream from the branch point has a similar function in splicing as it does in mammals [49]. Further studies using S. pombe are likely to provide insights into the mechanisms of splicing regulation fundamental to higher eukaryotes.…”

Section: Discussionsupporting

confidence: 79%

Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation

Tang

Käufer

Lin

2002

Biochemical Journal

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The unexpected low number of genes in the human genome has triggered increasing attention to alternative pre-mRNA splicing, and serine\arginine-rich (SR) proteins have been correlated with the complex alternative splicing that is a characteristic of metazoans. SR proteins interact with RNA and splicing protein factors, and they also undergo reversible phosphorylation, thereby regulating constitutive and alternative splicing in mammals and Drosophila. However, it is not clear whether the features of SR proteins and alternative splicing are present in simple and genetically tractable organisms, such as yeasts. In the present study, we show that the SR-like proteins Srp1 and Srp2, found in the fission yeast Schizosaccharomyces pombe, interact with each other and the interaction is modulated by protein phosphorylation. By using Srp1 as bait in a yeast two-hybrid

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Section: Discussionsupporting

confidence: 79%

Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation

Tang

Käufer

Lin

2002

Biochemical Journal

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“…The functional analysis localized complementing activity to a 3.0 kb SacI-EcoRI fragment, which we have sequenced in both directions. Three potential ORFs were identified which could be linked if two introns were postulated on the basis of the known consensus sequences for splicing in S.pombe (Prabhala et al, 1992). The intron structure of the radl 7 gene has been verified by PCR analysis and by the sequencing of a PCR product derived from cDNA that spans the region between base pairs 30 and 513 (see Materials and methods).…”

Section: Resultsmentioning

confidence: 99%

Fission yeast rad17: a homologue of budding yeast RAD24 that shares regions of sequence similarity with DNA polymerase accessory proteins.

et al. 1995

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contributed equally to this work 4Corresponding author Following DNA damage or a block to DNA synthesis, checkpoint pathways act to arrest mitosis and prevent the attempted segregation of damaged or unreplicated DNA. The radl7 locus of Schizosaccharomyces pombe is one of seven known radiation-sensitive (rad) loci which are absolutely required to prevent mitosis following DNA damage in fission yeast. Six of these (radi, rad3, rad9, radl 7, rad26 and husi) are also required for the checkpoint which prevents mitosis from occurring before DNA replication is complete. We report here that the predicted radl7 gene product is a basic hydrophilic protein of 606 amino acids which contains five domains with sequence homology to replication factor C (RF-C)/activator 1 subunits. Western analysis and fusion with Green Fluorescent Protein indicate that the abundance and electrophoretic mobility of Radl7 is not significantly modified following a block to DNA synthesis or following DNA damage, and that Radl7 is localized in the nucleus. Radl7 function is not essential for growth, but is required for the function of the DNA structure-dependent checkpoints. Sitedirected mutagenesis has been used to demonstrate the biological significance of the RF-C/activator 1-related domains. These studies have also defined an element of the radiation sensitivity caused by loss of Radl7 function which is not associated with the radiationinduced G2 arrest defect seen in the radl7.d null mutant cells.

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“…The pyrimidine rich region between the branch point and the 3' splice site is very similar between mammals and S. pombe although the latter is considerably shorter (Prabhala et al, 1992). Regarding the proteins involved in pre-mRNA processing humans and fission yeast have also many similarities.…”

Section: Alternative Splicingmentioning

confidence: 98%

Promoter-driven splicing regulation in fission yeast

Moldón

Malapeira

Gabrielli

et al. 2008

Nature

135

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AGRADECIMIENTOS vi viiDurante toda esta tesis veía clarísimo todo lo que escribir en este apartado y ahora que llega el momento me quedo en blanco... Debe ser la presión de saber que va a ser la sección más leída… Primero agradecer a José y a Elena el poder haber trabajado en este laboratorio durante este tiempo. Han sido casi dos tesis, sí, sí, mi primera página del cuaderno de laboratorio data del 19 de Abril del 2000, todavía recuerdo el primer día, lo primero que hice fue rotular eppendorfs con una temblorosa mano, cuántos nervios. Después de trabajar en muchos temas, momentos difíciles y agradables, odiosos y entrañables, mudanzas, meetings, reuniones, cenas y mil otros recuerdos que me llevo puedo decir que me va a costar estar lejos de este lugar. Un abrazo muy fuerte a los dos!! Mis compañeros de laboratorio, pasados, presentes y futuros, desde aquel chico de la UAB que me enseñó como utilizar una enzima de restricción hasta el chico nuevo que todavía no conozco... No tengo palabras. Habéis sido mi familia todo este tiempo:A la pequeña Ester que me ha cuidado desde el principio como una hermana mayor. A Ana con la que el odio y el cariño se entrelazaban continuamente, muy buena conversadora y con gran ojo crítico. A Carine cuya breve estancia me dejó entrever que hay más de una manera de hacer ciencia. A Jordi (MalaP), compañero de adversidades y aventuras. A Mercè, cuyo apoyo logístico y moral ha sido imprescindible. A Alice, símbolo de la ternura y de la filología italiana, ya se sabe, a caballo donato... A Miriam, una de las mejores personas que conozco, sensata, seria y muy inteligente, una gran científica. A Mónica, maestra de artes marciales y colis. A Blanca, la dulzura personificada y buen público para los chistes. A Nati, también compañera de poyata, penas y alegrías, una post-doc todavía sin título. A Isabel, la catol... una gran amiga y compañera de ChIPs, tranquila que las cosas se van arreglando solas! A Sarela, un meiga pero de las buenas y a Iván (el granaíno), que con su corta pero intensa estancia nos alegró las largas horas de laboratorio. A todos gracias por apoyarme, aguantarme y porque nadie mejor que vosotros sabe lo que supone esta tesis.Al resto de gente de la UPF, los vecinos de laboratorio, especialmente el laboratorio de Señalización Celular (o cariñosamente llamados "los posas") con los que hemos compartido más que un laboratorio, Inmunología (Mari, Bea, Mingui, Julia, Rosa, etc.), grandes amigos dentro y fuera de la UPF, y todos los demás grupos del departamento.Siguiendo la ampliación de espacio, gracias también a toda la gente del PRBB que han ayudado a que estos años se hicieran más amenos. Gracias a ellos se materializó viii la mejor terapia antiestrés, el voley, gracias a los Rabenessen de Caramel (incluido Iván, sí, podrás venir al pica pica de mi tesis, jeje).Gracias a mis compañeros de licenciatura, con ellos inicié este camino y espero seguir sendas cercanas a las suyas.A la gente del laboratorio de Paul Nurse en New York, gracias por haberme hecho pasar una de las m...

show abstract

Architectural features of pre‐mRNA introns in the fission yeast Schizosaccharmyces pombe

Cited by 87 publications

References 50 publications

Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation

Interactions between two fission yeast serine/arginine-rich proteins and their modulation by phosphorylation

Fission yeast rad17: a homologue of budding yeast RAD24 that shares regions of sequence similarity with DNA polymerase accessory proteins.

Promoter-driven splicing regulation in fission yeast

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