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- EMDB-4728: Cryo-EM structure of a poly(A) RNP bound to the Pan2-Pan3 deadenylase -

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Basic information

Entry
Database: EMDB / ID: EMD-4728
TitleCryo-EM structure of a poly(A) RNP bound to the Pan2-Pan3 deadenylase
Map datain publication (see figure S4): Map1, "full/complete map"
Sample
  • Complex: Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA
    • Complex: Pan2-Pan3
      • Protein or peptide: PAN2-PAN3 deadenylation complex catalytic subunit PAN2
      • Protein or peptide: PAN2-PAN3 deadenylation complex subunit PAN3
      • Protein or peptide: PAN2-PAN3 deadenylation complex subunit PAN3
    • Complex: Polyadenylate-binding protein, cytoplasmic and nuclear
      • Protein or peptide: Polyadenylate-binding protein, cytoplasmic and nuclear
    • Complex: RNA
      • RNA: poly(A) RNA
  • Ligand: MAGNESIUM ION
Function / homology
Function and homology information


regulation of nuclear-transcribed mRNA poly(A) tail shortening / ribonuclease inhibitor activity / PAN complex / poly(A)-specific ribonuclease / poly(A)-specific ribonuclease activity / nuclear-transcribed mRNA poly(A) tail shortening / poly(A) binding / postreplication repair / poly(U) RNA binding / regulation of translational initiation ...regulation of nuclear-transcribed mRNA poly(A) tail shortening / ribonuclease inhibitor activity / PAN complex / poly(A)-specific ribonuclease / poly(A)-specific ribonuclease activity / nuclear-transcribed mRNA poly(A) tail shortening / poly(A) binding / postreplication repair / poly(U) RNA binding / regulation of translational initiation / Translation initiation complex formation / intracellular non-membrane-bounded organelle / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / L13a-mediated translational silencing of Ceruloplasmin expression / mRNA transport / molecular condensate scaffold activity / mRNA 3'-UTR binding / promoter-specific chromatin binding / P-body / mRNA processing / cytoplasmic stress granule / nucleic acid binding / ribosome / protein kinase activity / ribonucleoprotein complex / DNA repair / mRNA binding / RNA binding / ATP binding / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
PAN2-PAN3 deadenylation complex subunit PAN3 / Pan3 pseudokinase domain / Pan3 Pseudokinase domain / PAN2, UCH domain / PAN2-PAN3 deadenylation complex catalytic subunit PAN2 / : / Ubiquitin carboxyl-terminal hydrolase / PAN2 N-terminal / : / PABP, RNA recognition motif 2 ...PAN2-PAN3 deadenylation complex subunit PAN3 / Pan3 pseudokinase domain / Pan3 Pseudokinase domain / PAN2, UCH domain / PAN2-PAN3 deadenylation complex catalytic subunit PAN2 / : / Ubiquitin carboxyl-terminal hydrolase / PAN2 N-terminal / : / PABP, RNA recognition motif 2 / Polyadenylate binding protein, human types 1, 2, 3, 4 / Polyadenylate-binding protein/Hyperplastic disc protein / Poly-adenylate binding protein, unique domain / Poly(A)-binding protein C-terminal (PABC) domain profile. / C-terminal domain of Poly(A)-binding protein. Present also in Drosophila hyperplastics discs protein. / PABC (PABP) domain / Exonuclease / RNA recognition motif domain, eukaryote / RNA recognition motif / Exonuclease, RNase T/DNA polymerase III / EXOIII / Zinc finger, CCCH-type / Zinc finger C3H1-type profile. / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Quinoprotein alcohol dehydrogenase-like superfamily / Papain-like cysteine peptidase superfamily / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Nucleotide-binding alpha-beta plait domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Polyadenylate-binding protein, cytoplasmic and nuclear / PAN2-PAN3 deadenylation complex subunit PAN3 / PAN2-PAN3 deadenylation complex catalytic subunit PAN2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Saccharomyces cerevisiae S288C (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.8 Å
AuthorsSchaefer IB / Conti E
CitationJournal: Cell / Year: 2019
Title: Molecular Basis for poly(A) RNP Architecture and Recognition by the Pan2-Pan3 Deadenylase.
Authors: Ingmar B Schäfer / Masami Yamashita / Jan Michael Schuller / Steffen Schüssler / Peter Reichelt / Mike Strauss / Elena Conti /
Abstract: The stability of eukaryotic mRNAs is dependent on a ribonucleoprotein (RNP) complex of poly(A)-binding proteins (PABPC1/Pab1) organized on the poly(A) tail. This poly(A) RNP not only protects mRNAs ...The stability of eukaryotic mRNAs is dependent on a ribonucleoprotein (RNP) complex of poly(A)-binding proteins (PABPC1/Pab1) organized on the poly(A) tail. This poly(A) RNP not only protects mRNAs from premature degradation but also stimulates the Pan2-Pan3 deadenylase complex to catalyze the first step of poly(A) tail shortening. We reconstituted this process in vitro using recombinant proteins and show that Pan2-Pan3 associates with and degrades poly(A) RNPs containing two or more Pab1 molecules. The cryo-EM structure of Pan2-Pan3 in complex with a poly(A) RNP composed of 90 adenosines and three Pab1 protomers shows how the oligomerization interfaces of Pab1 are recognized by conserved features of the deadenylase and thread the poly(A) RNA substrate into the nuclease active site. The structure reveals the basis for the periodic repeating architecture at the 3' end of cytoplasmic mRNAs. This illustrates mechanistically how RNA-bound Pab1 oligomers act as rulers for poly(A) tail length over the mRNAs' lifetime.
History
DepositionMar 25, 2019-
Header (metadata) releaseMay 29, 2019-
Map releaseMay 29, 2019-
UpdateDec 18, 2019-
Current statusDec 18, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.014
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.014
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  • Surface view with fitted model
  • Atomic models: PDB-6r5k
  • Surface level: 0.014
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4728.png

Downloads & links

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Map

FileDownload / File: emd_4728.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationin publication (see figure S4): Map1, "full/complete map"
Voxel sizeX=Y=Z: 1.056 Å
Density
Contour LevelBy AUTHOR: 0.014 / Movie #1: 0.014
Minimum - Maximum-0.012846572 - 0.051474016
Average (Standard dev.)0.00014905825 (±0.0026519466)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 304.128 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0561.0561.056
M x/y/z288288288
origin x/y/z0.0000.0000.000
length x/y/z304.128304.128304.128
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS288288288
D min/max/mean-0.0130.0510.000

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Supplemental data

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Mask #1

Fileemd_4728_msk_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Additional map: in publication (see figure S4): Map3, "map focused...

Fileemd_4728_additional_1.map
Annotationin publication (see figure S4): Map3, "map focused on RNase/RRM1 - RRM2 interaction"
Projections & Slices
AxesZYX

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Additional map: in publication (see figure S4): Map2, "map focused...

Fileemd_4728_additional_2.map
Annotationin publication (see figure S4): Map2, "map focused on recognition of Pab1 - Pab1 oligomerisation"
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Half map: independent halfmap 1 used for postprocessing of Map1

Fileemd_4728_half_map_1.map
Annotationindependent halfmap_1 used for postprocessing of Map1
Projections & Slices
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Half map: independent halfmap 2 used for postprocessing of Map1

Fileemd_4728_half_map_2.map
Annotationindependent halfmap_2 used for postprocessing of Map1
Projections & Slices
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Sample components

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Entire : Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA

EntireName: Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA
Components
  • Complex: Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA
    • Complex: Pan2-Pan3
      • Protein or peptide: PAN2-PAN3 deadenylation complex catalytic subunit PAN2
      • Protein or peptide: PAN2-PAN3 deadenylation complex subunit PAN3
      • Protein or peptide: PAN2-PAN3 deadenylation complex subunit PAN3
    • Complex: Polyadenylate-binding protein, cytoplasmic and nuclear
      • Protein or peptide: Polyadenylate-binding protein, cytoplasmic and nuclear
    • Complex: RNA
      • RNA: poly(A) RNA
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA

SupramoleculeName: Ternary Complex of Pan2-Pan3, Pab1 and poly(A) RNA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Molecular weightTheoretical: 498 KDa

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Supramolecule #2: Pan2-Pan3

SupramoleculeName: Pan2-Pan3 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1, #4-#5
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)

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Supramolecule #3: Polyadenylate-binding protein, cytoplasmic and nuclear

SupramoleculeName: Polyadenylate-binding protein, cytoplasmic and nuclear
type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)

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Supramolecule #4: RNA

SupramoleculeName: RNA / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Recombinant expressionOrganism: synthetic construct (others)

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Macromolecule #1: PAN2-PAN3 deadenylation complex catalytic subunit PAN2

MacromoleculeName: PAN2-PAN3 deadenylation complex catalytic subunit PAN2
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: poly(A)-specific ribonuclease
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 127.186602 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY GCISSYDPTF QLYTRYRGHI GGNSVKDILS HRDGILSIS EDSLHFANRR GVTKLNLTSI DIAAFSELNT MCYSPHSLKN NIYCGGDNTN WGIASIDLNR GCLDSLLNYS S KVKLMCSN ...String:
MNNWQHFFNN PVDLSEHLKK PYFRFDNRDK EITAISFDEK ANLIWSGDSY GCISSYDPTF QLYTRYRGHI GGNSVKDILS HRDGILSIS EDSLHFANRR GVTKLNLTSI DIAAFSELNT MCYSPHSLKN NIYCGGDNTN WGIASIDLNR GCLDSLLNYS S KVKLMCSN NKVLSIGRQT GTVDLLDPTS NRTIKSFNAH SASISAMDLR DNTLVTVGKS KRFYNLYADP FVNVYDLRTM RQ LPPVSFS KGTTMGSGGA DFVQLHPLLP TVMIVASSSG SFDFIDLSNP TLRTQYVHPC QSIKKLCLSP NGDVLGILEA DNH LDTWRR SSNNMGMFTN TPEMLAYPDY FNDITSDGPI SVDDETYPLS SVGMPYYLDK LLSAWPPVVF KSEGTIPQLT GKSP LPSSG KLKSNLAVIS SQNEKLSTQE FPLLRYDRTK YGMRNAIPDY VCLRDIRKQI TSGLETSDIQ TYTSINKYEV PPAYS RLPL TSGRFGTDNF DFTPFNNTEY SGLDPDVDNH YTNAIIQLYR FIPEMFNFVV GCLKDENFET TLLTDLGYLF DMMERS HGK ICSSSNFQAS LKSLTDKRQL ENGEPQEHLE EYLESLCIRE SIEDFNSSES IKRNMPQKFN RFLLSQLIKE EAQTVNH NI TLNQCFGLET EIRTECSCDH YDTTVKLLPS LSISGINKTV IKQLNKKSNG QNILPYIEYA MKNVTQKNSI CPTCGKTE T ITQECTVKNL PSVLSLELSL LDTEFSNIRS SKNWLTSEFY GSIIKNKAVL RSTASELKGT SHIFKYELNG YVAKITDNN NETRLVTYVK KYNPKENCFK WLMFNDYLVV EITEEEALKM TYPWKTPEII IYCDAEELRK PFFSVDTYSI NYDILFRDYF ANGIRDTAR REYKLLTHDE APKSGTLVAI DAEFVSLQSE LCEIDHQGIR SIIRPKRTAL ARISIIRGEE GELYGVPFVD D YVVNTNHI EDYLTRYSGI LPGDLDPEKS TKRLVRRNVV YRKVWLLMQL GCVFVGHGLN NDFKHININV PRNQIRDTAI YF LQGKRYL SLRYLAYVLL GMNIQEGNHD SIEDAHTALI LYKKYLHLKE KAIFEKVLNS VYEEGRAHNF KVPETSKG

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Macromolecule #2: Polyadenylate-binding protein, cytoplasmic and nuclear

MacromoleculeName: Polyadenylate-binding protein, cytoplasmic and nuclear
type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 64.778363 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: GPDSMADITD KTAEQLENLN IQDDQKQAAT GSESQSVENS SASLYVGDLE PSVSEAHLYD IFSPIGSVSS IRVCRDAITK TSLGYAYVN FNDHEAGRKA IEQLNYTPIK GRLCRIMWSQ RDPSLRKKGS GNIFIKNLHP DIDNKALYDT FSVFGDILSS K IATDENGK ...String:
GPDSMADITD KTAEQLENLN IQDDQKQAAT GSESQSVENS SASLYVGDLE PSVSEAHLYD IFSPIGSVSS IRVCRDAITK TSLGYAYVN FNDHEAGRKA IEQLNYTPIK GRLCRIMWSQ RDPSLRKKGS GNIFIKNLHP DIDNKALYDT FSVFGDILSS K IATDENGK SKGFGFVHFE EEGAAKEAID ALNGMLLNGQ EIYVAPHLSR KERDSQLEET KAHYTNLYVK NINSETTDEQ FQ ELFAKFG PIVSASLEKD ADGKLKGFGF VNYEKHEDAV KAVEALNDSE LNGEKLYVGR AQKKNERMHV LKKQYEAYRL EKM AKYQGV NLFVKNLDDS VDDEKLEEEF APYGTITSAK VMRTENGKSK GFGFVCFSTP EEATKAITEK NQQIVAGKPL YVAI AQRKD VRRSQLAQQI QARNQMRYQQ ATAAAAAAAA GMPGQFMPPM FYGVMPPRGV PFNGPNPQQM NPMGGMPKNG MPPQF RNGP VYGVPPQGGF PRNANDNNQF YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ EVFPLLESDE LFEQHY KEA SAAYESFKKE QEQQTEQA

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Macromolecule #4: PAN2-PAN3 deadenylation complex subunit PAN3

MacromoleculeName: PAN2-PAN3 deadenylation complex subunit PAN3 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 53.218609 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MHSLLQYHIS LYAPEQPSSL KSLLKPNERS ADQLFIPNNI REDLTKKNLS ILQVFPSSGK VIPSIVQDYF NLVPLNFNNN DFLNKTTLF KVFSNYDGKA YVLKRLPNID KSMNPNKISK IYQIWSKINC TNLIKFRDIF QTTKFGNLSI CLVFDYYPNS L SLYDYHFV ...String:
MHSLLQYHIS LYAPEQPSSL KSLLKPNERS ADQLFIPNNI REDLTKKNLS ILQVFPSSGK VIPSIVQDYF NLVPLNFNNN DFLNKTTLF KVFSNYDGKA YVLKRLPNID KSMNPNKISK IYQIWSKINC TNLIKFRDIF QTTKFGNLSI CLVFDYYPNS L SLYDYHFV NFPKFPITNN YLWIYLVQLT NVINSIHSQN LSIGNTLNWR KVLITGDPGR IKLSHCNFMD LLFNDDTDTV VS SGGSTIE GQQQLDYKYL GELLFNLSIN IENSNNNTAP KEYRLEEITP QSIDDMRQID DKFKDVLKYL ISDNGDSKKS IHD LTSHFY DKMFMVLESS QTYTEYMESV LSRELENGRL FRLVNKLNCI FGRIESRIDI NWSESGTKFP IILFYDYVFH QVDS NGKPI MDLTHVLRCL NKLDAGIQEK LMLVTPDELN CIIISYKQLK DLIESTFRSI TQA

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Macromolecule #5: PAN2-PAN3 deadenylation complex subunit PAN3

MacromoleculeName: PAN2-PAN3 deadenylation complex subunit PAN3 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 77.906688 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI DVGEATTPTM TSVPKFNAKV SASFTPMTVG SDSLTTVTN TTSAATNATG NIAMAATSAT ASTVNPMINP IVNSSLVNNN NNNSNISISI PTTASSSNYD PFNAPIFTPS S TSSIHTNA ...String:
MDKINPDWAK DIPCRNITIY GYCKKEKEGC PFKHSDNTTA TTINDVPPPI DVGEATTPTM TSVPKFNAKV SASFTPMTVG SDSLTTVTN TTSAATNATG NIAMAATSAT ASTVNPMINP IVNSSLVNNN NNNSNISISI PTTASSSNYD PFNAPIFTPS S TSSIHTNA NAHSFPFPSI ANSGGININA TDDNSNNMSM ANNVPPPMQP PPIESSNLKY PRIYPPPHSL LQYHLYAPEQ PS SLKSLLK PNERSADQLF IPNNIREDLT KKNLSILQVF PSSGKVIPSI VQDYFNLVPL NFNNNDFLNK TTLFKVFSNY DGK AYVLKR LPNIDKSMNP NKISKIYQIW SKINCTNLIK FRDIFQTTKF GDLSICLVFD YYPNSLSLYD YHFVNFPKFP ITNN YLWIY LVQLTNVINS IHSQNLSIGN TLNWRKVLIT GDPGRIKLSH CNFMDLLFND DTDTVVSSGG STIEGQQQLD YKYLG ELLF NLSINIENSN NNTAPKEYRL EEITPQSIDD MRQIDDKFKD VLKYLISDNG DSKKSIHDLT SHFYDKMFMV LESSQT YTE YMESVLSREL ENGRLFRLVN KLNCIFGRIE SRIDINWSES GTKFPIILFY DYVFHQVDSN GKPIMDLTHV LRCLNKL DA GIQEKLMLVT PDELNCIIIS YKELKDLIES TFRSITQHHH HHHHHHH

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Macromolecule #3: poly(A) RNA

MacromoleculeName: poly(A) RNA / type: rna / ID: 3 / Number of copies: 1
Source (natural)Organism: Saccharomyces cerevisiae S288C (yeast)
Molecular weightTheoretical: 29.583547 KDa
SequenceString:
AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAA A

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Macromolecule #6: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 6 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Pressure: 0.022 kPa
VitrificationCryogen name: ETHANE-PROPANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Sampling interval: 5.0 µm / Digitization - Frames/image: 2-40 / Number grids imaged: 1 / Number real images: 6463 / Average exposure time: 8.0 sec. / Average electron dose: 51.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 2141230
CTF correctionSoftware - Name: Gctf (ver. 1.06)
Startup modelType of model: INSILICO MODEL
In silico model: prepared using sxviper (Penczek et al., 1994)
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0-beta-1)
Final 3D classificationNumber classes: 8 / Avg.num./class: 30000 / Software - Name: RELION (ver. 3.0-beta-1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 3.0-beta-1)
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0-beta-1) / Number images used: 29165

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: RIGID BODY FIT / Overall B value: 45.7 / Target criteria: Cross-correlation coefficient
Output model

PDB-6r5k:
Cryo-EM structure of a poly(A) RNP bound to the Pan2-Pan3 deadenylase

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