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Protein

Guanyl-specific ribonuclease pgl-1

Gene

pgl-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). Together with the P-granule component pgl-3, is involved in the formation of P-granules (PubMed:21402787, PubMed:24746798). Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules (PubMed:21402787). In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (PubMed:26598553). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (PubMed:26598553). May protect somatic cells from excessive apoptosis during normal development (PubMed:27650246). Essential role in male and female postembryonic germline development; maternally provided protein maintains a population of proliferating germ cells and zygotic expression is required for correct oogenesis (PubMed:9741628, PubMed:15238518, PubMed:24746798).7 Publications

Catalytic activityi

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.1 Publication

Cofactori

Note: Does not require metal ions for catalytic activity.1 Publication

Enzyme regulationi

Not inhibited by RNase inhibitor RNasin.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei437Proton acceptor1 Publication1

GO - Molecular functioni

  • ATP-dependent RNA helicase activity Source: GO_Central
  • endonuclease activity Source: UniProtKB-KW
  • protein self-association Source: WormBase
  • ribonuclease T1 activity Source: UniProtKB-EC
  • RNA binding Source: WormBase

GO - Biological processi

  • gamete generation Source: WormBase
  • germ-line stem cell division Source: WormBase
  • oogenesis Source: WormBase
  • P granule organization Source: WormBase
  • reproduction Source: WormBase
  • RNA secondary structure unwinding Source: GO_Central

Keywordsi

Molecular functionDevelopmental protein, Endonuclease, Hydrolase, Nuclease, RNA-binding
Biological processDifferentiation, Oogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Guanyl-specific ribonuclease pgl-1Curated (EC:3.1.27.31 Publication)
Alternative name(s):
P granule abnormality protein 1
Gene namesi
Name:pgl-1Imported
ORF Names:ZK381.4Imported
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiZK381.4a ; CE25689 ; WBGene00003992 ; pgl-1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Pathology & Biotechi

Disruption phenotypei

Temperature-sensitive and are only fertile at 20 degrees Celsius (PubMed:26787882). 25% of progeny arresting as late embryos and 9% as larvae at 26 degrees Celsius (PubMed:15238518). Surviving progeny are sterile at 26 degrees Celsius, most likely due to germline proliferation defects (PubMed:9741628, PubMed:15238518, PubMed:26787882). The temperature-sensitive period extends from mid-larvae to young adults (PubMed:9741628). Germline defects include increased apoptosis in the gonad, fewer germ nuclei, no sperm and no oocytes in the gonad arms (PubMed:15238518, PubMed:26598553). Double knockout with pgl-3 results in 37% of progeny arresting as late embryos and 9% as larvae at 26 degrees Celsius (PubMed:15238518). Double knockout with pgl-3 enhances the temperature-sensitive sterility phenotype and germline defects of the pgl-1 single knockout (PubMed:15238518, PubMed:26598553). The gonads of the double knockout with pgl-3 degenerate as the adults age (PubMed:15238518). Triple knockout with pgl-2 and pgl-3 results in 58% of progeny arresting as late embryos and 5% as larvae at 26 degrees Celsius (PubMed:15238518). Double knockout with him-3 decreases the number of self-cross progeny in the him-3 single mutant (PubMed:15238518). Triple knockout with pgl-3 and him-3 further reduces the number of self-cross progeny as compared to the pgl-1 and him-3 double mutant and him-3 single mutant (PubMed:15238518). Double knockout with ced-1 results in an increased number of cell corpses in the gonad as compared to the ced-1 single mutant (PubMed:26598553). Conversely, double knockout with ced-1 results in reduced somatic cell apoptosis (PubMed:27650246). Triple knockout with ced-1 and hpl-2 partially recovers the reduced somatic cell apoptotic cell defect in the ced-1 and hpl-2 double knockout (PubMed:27650246). Triple knockout with ced-1 and hpl-2 and knockdown with either ced-3 or ced-4 reduces the somatic cell apoptosis defect in the ced-1, hpl-2 and pgl-1 triple knockout (PubMed:27650246). Double RNAi-mediated knockdown with pgl-1 results in a reduced number of pos-1, mex-1 and glh-1 positive granules in embryos (PubMed:21402787). Quadruple RNAi-mediated knockdown with glh-1, glh-4 and pgl-3 results in offspring that display 27-89% sterility, abnormal oocytes and do not have embryos in the uterus (PubMed:24746798). These sterile offspring still produce sperm (PubMed:24746798). Furthermore, these offspring may have compromised P-granule integrity as there is diffuse cytoplasmic localization of the P-granule component deps-1, which may cause germ cells to initiate somatic reprogramming (PubMed:24746798). RNAi-mediated knockdown in a double ced-1 and hpl-2 mutant background rescues the reduced somatic cell apoptotic cell defect in the ced-1 and hpl-2 double knockout (PubMed:27650246).7 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi301Q → A: Abolished catalytic activity. No effect on dimerization or RNA-binding. 1 Publication1
Mutagenesisi401E → Q: No effect on catalytic activity. 1 Publication1
Mutagenesisi437H → A: Reduced catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000583571 – 730Guanyl-specific ribonuclease pgl-1Add BLAST730

Post-translational modificationi

Methylated at arginine residues in the RNA-binding RGG-box by prmt-1. Methylation promotes P-granule degradation by autophagy.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

EPDiQ9TZQ3
PaxDbiQ9TZQ3
PRIDEiQ9TZQ3

Expressioni

Tissue specificityi

Expressed in the germline (PubMed:9741628, PubMed:15238518). Expressed in most somatic cells (PubMed:27650246).3 Publications

Developmental stagei

Expressed throughout development from embryos to adults (PubMed:9741628, PubMed:15238518, PubMed:27650246). Not expressed in somatic cells of embryos (PubMed:28806108). First expressed in 1-cell embryos, and expression persists until the 4-cell stage (PubMed:15238518). Expression diminishes in somatic blastomeres, but remains in E and P3 blastomeres at the 8-cell stage, in P3 blastomeres at the 15-cell stage, and in P4 blastomeres at the 24-cell stage (PubMed:15238518). Expressed in the primordial germ cells Z2 and Z3 during the two-fold stage of embryogenesis (PubMed:15238518, PubMed:27650246). Levels are low in young larvae but increase at the end of larval development (PubMed:9741628). Expressed in germ blastomeres (PubMed:19377305).5 Publications

Gene expression databases

BgeeiWBGene00003992
ExpressionAtlasiQ9TZQ3 baseline and differential

Interactioni

Subunit structurei

Homodimer (PubMed:15238518, PubMed:26787882). Interacts with pgl-2 and pgl-3; this association is not required for P-granule localization of either pgl-2 or pgl-3 (PubMed:15238518). Interacts with ife-1 (PubMed:11641215, PubMed:15238518). Interacts with prmt-1; the interaction is direct (PubMed:24140420).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ife-1O455512EBI-332200,EBI-330148

GO - Molecular functioni

  • protein self-association Source: WormBase

Protein-protein interaction databases

BioGridi42581, 4 interactors
DIPiDIP-26042N
IntActiQ9TZQ3, 2 interactors
STRINGi6239.ZK381.4b

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5CV1X-ray3.60A205-447[»]
ProteinModelPortaliQ9TZQ3
SMRiQ9TZQ3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni205 – 447Involved in dimerization1 PublicationAdd BLAST243
Regioni674 – 730RNA-binding RGG-box1 PublicationAdd BLAST57

Domaini

The dimerization domain also acts as a hinge; changes in its structure probably impact oligomerization and RNA-binding.1 Publication
The RNA-binding RGG-box is required for the recruitment of some P-granule components such as pos-1 and probably mRNA, but is dispensable for granule formation.1 Publication1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410KABH Eukaryota
ENOG4110IF4 LUCA
GeneTreeiENSGT00390000008064
HOGENOMiHOG000017375
InParanoidiQ9TZQ3

Sequencei

Sequence statusi: Complete.

Q9TZQ3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEANKREIVD FGGLRSYFFP NLAHYITKND EELFNNTSQA NKLAAFVLGA
60 70 80 90 100
SKDAPGDEDI LEMILPNDAN AAVIAAGMDV CLLLGDKFRP KFDAAAEKLS
110 120 130 140 150
GLGHAHDLVS VIDDDKKLGM LARKAKLKKT EDAKILQALL KVIAIDDAAE
160 170 180 190 200
KFVELTELVS QLDLDFDVYV LTKILGLISE ETSDEVDIIR DNVVNAFDSC
210 220 230 240 250
KPLLKQLMLD GPKSEPADPF ISLLMDPLEE SVGKVVNHIA QLFEEASKNE
260 270 280 290 300
GDESLVLRSQ LGYQLFFLIV RSLADGKREV SKKILSGIPT SVRAEVFPGL
310 320 330 340 350
QRSVYKSAVF LGNHIIQVLL GSKKSFEDWD VVGVAKDLES AWKRRAIAEL
360 370 380 390 400
IKKFQVSILE QCFDKPVPLI PQSPLNNDAV IDNVNKALQF ALWLTEFYGS
410 420 430 440 450
ENETEALGEL RFLDSTSKNL LVDSFKKFVQ GINSKTHVTR IVESLEKCCL
460 470 480 490 500
SDTPSGRKSN VQPSTSQQQD SAYTKEEMTT VHNTYSVNTK AQVLNGLSDT
510 520 530 540 550
NSSGLLVDSK DSLSLQEISC DEVDSSTLLS SSRNIGEGVT VKAVDPVPEK
560 570 580 590 600
VNDAQQQQTV NEIEMASDAN QDTSSSASPE VAPSFSTDGW DSPTKSVALP
610 620 630 640 650
PGMQQIDEEE TTVADKDSTP QPQARAETAW GSGDATPMPL PAPTNQYKVS
660 670 680 690 700
GFGEAKVAKG FGQFAPTSSA YGGGGGRGGY GGGDRGGRGG YGGDRGGRGG
710 720 730
YGGGDRGGRG GYGGDRGRGG YGGRGGRGGF
Length:730
Mass (Da):78,454
Last modified:May 1, 2000 - v1
Checksum:i779FFC6180376D7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077868 mRNA Translation: AAC36100.1
FO080210 Genomic DNA Translation: CCD62010.1
PIRiT43317
RefSeqiNP_001041065.1, NM_001047600.3
UniGeneiCel.23408

Genome annotation databases

EnsemblMetazoaiZK381.4a.1; ZK381.4a.1; WBGene00003992
ZK381.4a.2; ZK381.4a.2; WBGene00003992
GeneIDi177461
UCSCiZK381.4a.1 c. elegans

Similar proteinsi

Entry informationi

Entry nameiPGL1_CAEEL
AccessioniPrimary (citable) accession number: Q9TZQ3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 105 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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