Lsm1-7-Pat1 complex:  A link between 3’ and 5’-ends in mRNA decay?

Tharun, Sundaresan

doi:10.4161/rna.6.3.8282

Cited by 49 publications

(50 citation statements)

References 45 publications

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“…Pat1p is thought to recruit the LSm1-7 complex to P-bodies in order to trigger decapping [15] (Figure 1). The purified LSm1-7-Pat1 complex binds preferentially at the 3 -end of oligoadenylated mRNAs rather than polyadenylated mRNAs [3,[19][20][21]. Furthermore, the LSm1-7-Pat1 complex interacts with the decapping complex, Dcp1/2, in an RNAdependent manner, probably via deadenylated mRNAs [3].…”

Section: Yeast Pat1p and 5 →3 Mrna Decaymentioning

confidence: 99%

Pat1 proteins: a life in translation, translation repression and mRNA decay

Marnef

Standart

2010

Biochemical Society Transactions

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Pat1 proteins are conserved across eukaryotes. Vertebrates have evolved two Pat1 proteins paralogues, whereas invertebrates and yeast only possess one such protein. Despite their lack of known domains or motifs, Pat1 proteins are involved in several key post-transcriptional mechanisms of gene expression control. In yeast, Pat1p interacts with translating mRNPs (messenger ribonucleoproteins), and is responsible for translational repression and decapping activation, ultimately leading to mRNP degradation. Drosophila HPat and human Pat1b (PatL1) proteins also have conserved roles in the 5'→3' mRNA decay pathway. Consistent with their functions in silencing gene expression, Pat1 proteins localize to P-bodies (processing bodies) in yeast, Drosophila, Caenorhabditis elegans and human cells. Altogether, Pat1 proteins may act as scaffold proteins allowing the sequential binding of repression and decay factors on mRNPs, eventually leading to their degradation. In the present mini-review, we present the current knowledge on Pat1 proteins in the context of their multiple functions in post-transcriptional control.

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Section: Yeast Pat1p and 5 →3 Mrna Decaymentioning

confidence: 99%

Pat1 proteins: a life in translation, translation repression and mRNA decay

Marnef

Standart

2010

Biochemical Society Transactions

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“…In yeast and metazoa, the heptameric LSM1-7 complex, in association with PROTEIN-ASSOCIATED WITH TOPOISOMERASE1 (PAT1), binds to the 39 end of deadenylated mRNAs and promotes decapping (Tharun, 2009;Haas et al, 2010). Simultaneously, PAT1 interacts with the DEAD-box RNA helicase DHH1/ DDX6.…”

Section: Decappingmentioning

confidence: 99%

Polysomes, Stress Granules, and Processing Bodies: A Dynamic Triumvirate Controlling Cytoplasmic mRNA Fate and Function

2017

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“…The cytoplasmically localized heterooctameric Lsm1-7-Pat1 complex made up of the seven Smlike proteins (Lsm1 through Lsm7) and the Pat1 protein conserved in all eukaryotes is a key activator of the decapping enzyme and is essential for the normal rates of mRNA decapping in vivo (Bouveret et al 2000;Tharun et al 2000;Tharun 2009b;Totaro et al 2011). This complex also protects mRNA 3 ′ -ends from trimming (Boeck et al 1998;He and Parker 2001;Tharun et al 2005;Tharun 2009a). Consistent with its role in activation of deadenylation-dependent decapping in the 5 ′ -to-3 ′ pathway and in the protection of mRNA 3 ′ -ends, the Lsm1-7-Pat1 complex purified from yeast has RNA binding activity, exhibits a unique binding preference for oligoadenylated RNAs over polyadenylated RNAs, and binds at the 3 ′ -ends of RNAs (Chowdhury et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex

Chowdhury

Kalurupalle

Tharun

2014

RNA

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A major mRNA decay pathway in eukaryotes is initiated by deadenylation followed by decapping of the oligoadenylated mRNAs and subsequent 5 ′ -to-3 ′ exonucleolytic degradation of the capless mRNA. In this pathway, decapping is a rate-limiting step that requires the hetero-octameric Lsm1-7-Pat1 complex to occur at normal rates in vivo. This complex is made up of the seven Sm-like proteins, Lsm1 through Lsm7, and the Pat1 protein. It binds RNA and has a unique binding preference for oligoadenylated RNAs over polyadenylated RNAs. Such binding ability is crucial for its mRNA decay function in vivo. In order to determine the contribution of Pat1 to the function of the Lsm1-7-Pat1 complex, we compared the RNA binding properties of the Lsm1-7 complex purified from pat1Δ cells and purified Pat1 fragments with that of the wild-type Lsm1-7-Pat1 complex. Our studies revealed that both the Lsm1-7 complex and purified Pat1 fragments have very low RNA binding activity and are impaired in the ability to recognize the oligo(A) tail on the RNA. However, reconstitution of the Lsm1-7-Pat1 complex from these components restored these abilities. We also observed that Pat1 directly contacts RNA in the context of the Lsm1-7-Pat1 complex. These studies suggest that the unique RNA binding properties and the mRNA decay function of the Lsm1-7-Pat1 complex involve cooperation of residues from both Pat1 and the Lsm1-7 ring. Finally our studies also revealed that the middle domain of Pat1 is essential for the interaction of Pat1 with the Lsm1-7 complex in vivo.

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Lsm1-7-Pat1 complex: A link between 3’ and 5’-ends in mRNA decay?

Abstract: To cite this article: Sundaresan Tharun (2009) Lsm1-7-Pat1 complex: A link between 3' and 5'-ends in mRNA decay?, RNA Biology, 6:3,[228][229][230][231][232]

Cited by 49 publications

References 45 publications

Pat1 proteins: a life in translation, translation repression and mRNA decay

Pat1 proteins: a life in translation, translation repression and mRNA decay

Polysomes, Stress Granules, and Processing Bodies: A Dynamic Triumvirate Controlling Cytoplasmic mRNA Fate and Function

Pat1 contributes to the RNA binding activity of the Lsm1-7–Pat1 complex

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