• Je něco špatně v tomto záznamu ?

A unique mRNA decapping complex in trypanosomes

S. Kramer, NK. Karolak, J. Odenwald, B. Gabiatti, PA. Castañeda Londoño, A. Zavřelová, ER. Freire, KS. Almeida, S. Braune, C. Moreira, A. Eder, C. Goos, M. Field, M. Carrington, F. Holetz, MW. Górna, M. Zoltner

. 2023 ; 51 (14) : 7520-7540. [pub] 2023Aug11

Jazyk angličtina Země Anglie, Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc23016587

Grantová podpora
217138/Z/19/Z Wellcome Trust - United Kingdom
204697/Z/16/Z Wellcome Trust - United Kingdom
097945/B/11/Z Wellcome Trust - United Kingdom

Removal of the mRNA 5' cap primes transcripts for degradation and is central for regulating gene expression in eukaryotes. The canonical decapping enzyme Dcp2 is stringently controlled by assembly into a dynamic multi-protein complex together with the 5'-3'exoribonuclease Xrn1. Kinetoplastida lack Dcp2 orthologues but instead rely on the ApaH-like phosphatase ALPH1 for decapping. ALPH1 is composed of a catalytic domain flanked by C- and N-terminal extensions. We show that T. brucei ALPH1 is dimeric in vitro and functions within a complex composed of the trypanosome Xrn1 ortholog XRNA and four proteins unique to Kinetoplastida, including two RNA-binding proteins and a CMGC-family protein kinase. All ALPH1-associated proteins share a unique and dynamic localization to a structure at the posterior pole of the cell, anterior to the microtubule plus ends. XRNA affinity capture in T. cruzi recapitulates this interaction network. The ALPH1 N-terminus is not required for viability in culture, but essential for posterior pole localization. The C-terminus, in contrast, is required for localization to all RNA granule types, as well as for dimerization and interactions with XRNA and the CMGC kinase, suggesting possible regulatory mechanisms. Most significantly, the trypanosome decapping complex has a unique composition, differentiating the process from opisthokonts.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc23016587
003      
CZ-PrNML
005      
20231026105713.0
007      
ta
008      
231013s2023 enk f 000 0|eng||
009      
AR
024    7_
$a 10.1093/nar/gkad497 $2 doi
035    __
$a (PubMed)37309887
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a enk
100    1_
$a Kramer, Susanne $u Biocenter, University of Würzburg, Würzburg, Germany $1 https://orcid.org/0000000263022560
245    12
$a A unique mRNA decapping complex in trypanosomes / $c S. Kramer, NK. Karolak, J. Odenwald, B. Gabiatti, PA. Castañeda Londoño, A. Zavřelová, ER. Freire, KS. Almeida, S. Braune, C. Moreira, A. Eder, C. Goos, M. Field, M. Carrington, F. Holetz, MW. Górna, M. Zoltner
520    9_
$a Removal of the mRNA 5' cap primes transcripts for degradation and is central for regulating gene expression in eukaryotes. The canonical decapping enzyme Dcp2 is stringently controlled by assembly into a dynamic multi-protein complex together with the 5'-3'exoribonuclease Xrn1. Kinetoplastida lack Dcp2 orthologues but instead rely on the ApaH-like phosphatase ALPH1 for decapping. ALPH1 is composed of a catalytic domain flanked by C- and N-terminal extensions. We show that T. brucei ALPH1 is dimeric in vitro and functions within a complex composed of the trypanosome Xrn1 ortholog XRNA and four proteins unique to Kinetoplastida, including two RNA-binding proteins and a CMGC-family protein kinase. All ALPH1-associated proteins share a unique and dynamic localization to a structure at the posterior pole of the cell, anterior to the microtubule plus ends. XRNA affinity capture in T. cruzi recapitulates this interaction network. The ALPH1 N-terminus is not required for viability in culture, but essential for posterior pole localization. The C-terminus, in contrast, is required for localization to all RNA granule types, as well as for dimerization and interactions with XRNA and the CMGC kinase, suggesting possible regulatory mechanisms. Most significantly, the trypanosome decapping complex has a unique composition, differentiating the process from opisthokonts.
650    12
$a endoribonukleasy $x metabolismus $7 D004722
650    12
$a RNA čepičky $x genetika $x metabolismus $7 D012315
650    _2
$a stabilita RNA $7 D020871
650    _2
$a messenger RNA $x genetika $x metabolismus $7 D012333
650    _2
$a proteiny vázající RNA $x genetika $x metabolismus $7 D016601
650    12
$a Trypanosoma $x genetika $7 D014345
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Karolak, Natalia Katarzyna $u Biological and Chemical Research Centre, Department of Chemistry, University of Warsaw, Warsaw, Poland $u Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland
700    1_
$a Odenwald, Johanna $u Biocenter, University of Würzburg, Würzburg, Germany
700    1_
$a Gabiatti, Bernardo $u Biocenter, University of Würzburg, Würzburg, Germany $u Carlos Chagas Institute (ICC), FIOCRUZ/PR, Curitiba, Brazil
700    1_
$a Castañeda Londoño, Paula Andrea $u Biocenter, University of Würzburg, Würzburg, Germany
700    1_
$a Zavřelová, Anna $u Department of Parasitology, Faculty of Science, Charles University in Prague, Biocev, Vestec, Czech Republic
700    1_
$a Freire, Eden Ribeiro $u Carlos Chagas Institute (ICC), FIOCRUZ/PR, Curitiba, Brazil
700    1_
$a Almeida, Kayo Schemiko $u Carlos Chagas Institute (ICC), FIOCRUZ/PR, Curitiba, Brazil
700    1_
$a Braune, Silke $u Biocenter, University of Würzburg, Würzburg, Germany
700    1_
$a Moreira, Claudia $u Biocenter, University of Würzburg, Würzburg, Germany $u Carlos Chagas Institute (ICC), FIOCRUZ/PR, Curitiba, Brazil
700    1_
$a Eder, Amelie $u Biocenter, University of Würzburg, Würzburg, Germany
700    1_
$a Goos, Carina $u Biocenter, University of Würzburg, Würzburg, Germany
700    1_
$a Field, Mark $u School of Life Sciences, University of Dundee, Dundee, UK $u Biology Centre, Czech Academy of Sciences, Institute of Parasitology, České Budějovice, Czech Republic $1 https://orcid.org/0000000248662885
700    1_
$a Carrington, Mark $u Department of Biochemistry, University of Cambridge, Cambridge, UK $1 https://orcid.org/0000000264357266
700    1_
$a Holetz, Fabiola $u Carlos Chagas Institute (ICC), FIOCRUZ/PR, Curitiba, Brazil
700    1_
$a Górna, Maria Wiktoria $u Biological and Chemical Research Centre, Department of Chemistry, University of Warsaw, Warsaw, Poland
700    1_
$a Zoltner, Martin $u Department of Parasitology, Faculty of Science, Charles University in Prague, Biocev, Vestec, Czech Republic
773    0_
$w MED00003554 $t Nucleic acids research $x 1362-4962 $g Roč. 51, č. 14 (2023), s. 7520-7540
856    41
$u https://pubmed.ncbi.nlm.nih.gov/37309887 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y - $z 0
990    __
$a 20231013 $b ABA008
991    __
$a 20231026105707 $b ABA008
999    __
$a ok $b bmc $g 2000231 $s 1202949
BAS    __
$a 3
BAS    __
$a PreBMC-MEDLINE
BMC    __
$a 2023 $b 51 $c 14 $d 7520-7540 $e 2023Aug11 $i 1362-4962 $m Nucleic acids research $n Nucleic Acids Res $x MED00003554
GRA    __
$a 217138/Z/19/Z $p Wellcome Trust $2 United Kingdom
GRA    __
$a 204697/Z/16/Z $p Wellcome Trust $2 United Kingdom
GRA    __
$a 097945/B/11/Z $p Wellcome Trust $2 United Kingdom
LZP    __
$a Pubmed-20231013

Najít záznam

Citační ukazatele

    Možnosti archivace