New insights into trypanosomatid U5 small nuclear ribonucleoproteins
Main Author: | |
---|---|
Publication Date: | 2011 |
Other Authors: | , , , , , , , |
Format: | Article |
Language: | eng |
Source: | Memórias do Instituto Oswaldo Cruz |
Download full: | http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200003 |
Summary: | Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes. In this context, certain small complexes of RNA and protein, which are named small nuclear ribonucleoproteins (U snRNPs), have an essential role in pre-mRNA processing, mainly during splicing. Even though they are well defined in mammals, snRNPs are still not well characterized in trypanosomatids. This study shows that a U5-15K protein is highly conserved among various trypanosomatid species. Tandem affinity pull-down assays revealed that this protein interacts with a novel U5-102K protein, which suggests the presence of a sub-complex that is potentially involved in the assembly of U4/U6-U5 tri-snRNPs. Functional analyses showed that U5-15K is essential for cell viability and is somehow involved with the trans and cis splicing machinery. Similar tandem affinity experiments with a trypanonosomatid U5-Cwc21 protein led to the purification of four U5 snRNP specific proteins and a Sm core, suggesting U5-Cwc-21 participation in the 35S U5 snRNP particle. Of these proteins, U5-200K was molecularly characterized. U5-200K has conserved domains, such as the DEAD/DEAH box helicase and Sec63 domains and displays a strong interaction with U5 snRNA. |
id |
FIOCRUZ-4_4aa7c5d1fd00853a08c1a5414c38f7d8 |
---|---|
oai_identifier_str |
oai:scielo:S0074-02762011000200003 |
network_acronym_str |
FIOCRUZ-4 |
network_name_str |
Memórias do Instituto Oswaldo Cruz |
spelling |
New insights into trypanosomatid U5 small nuclear ribonucleoproteinstrans splicingcis splicingU5 snRNPU5-Cwc-21PTP-TagTrypanosoma cruziTrypanosoma bruceiSeveral protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes. In this context, certain small complexes of RNA and protein, which are named small nuclear ribonucleoproteins (U snRNPs), have an essential role in pre-mRNA processing, mainly during splicing. Even though they are well defined in mammals, snRNPs are still not well characterized in trypanosomatids. This study shows that a U5-15K protein is highly conserved among various trypanosomatid species. Tandem affinity pull-down assays revealed that this protein interacts with a novel U5-102K protein, which suggests the presence of a sub-complex that is potentially involved in the assembly of U4/U6-U5 tri-snRNPs. Functional analyses showed that U5-15K is essential for cell viability and is somehow involved with the trans and cis splicing machinery. Similar tandem affinity experiments with a trypanonosomatid U5-Cwc21 protein led to the purification of four U5 snRNP specific proteins and a Sm core, suggesting U5-Cwc-21 participation in the 35S U5 snRNP particle. Of these proteins, U5-200K was molecularly characterized. U5-200K has conserved domains, such as the DEAD/DEAH box helicase and Sec63 domains and displays a strong interaction with U5 snRNA.Instituto Oswaldo Cruz, Ministério da Saúde2011-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200003Memórias do Instituto Oswaldo Cruz v.106 n.2 2011reponame:Memórias do Instituto Oswaldo Cruzinstname:Fundação Oswaldo Cruzinstacron:FIOCRUZ10.1590/S0074-02762011000200003info:eu-repo/semantics/openAccessSilva,Marco Túlio A daAmbrósio,Daniela LTrevelin,Caroline CWatanabe,Tatiana FLaure,Helen JGreene,Lewis JRosa,José CValentini,Sandro RCicarelli,Regina MBeng2020-04-25T17:50:57Zhttp://www.scielo.br/oai/scielo-oai.php0074-02761678-8060opendoar:null2020-04-26 02:17:29.51Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruztrue |
dc.title.none.fl_str_mv |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
title |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
spellingShingle |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins Silva,Marco Túlio A da trans splicing cis splicing U5 snRNP U5-Cwc-21 PTP-Tag Trypanosoma cruzi Trypanosoma brucei |
title_short |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
title_full |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
title_fullStr |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
title_full_unstemmed |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
title_sort |
New insights into trypanosomatid U5 small nuclear ribonucleoproteins |
author |
Silva,Marco Túlio A da |
author_facet |
Silva,Marco Túlio A da Ambrósio,Daniela L Trevelin,Caroline C Watanabe,Tatiana F Laure,Helen J Greene,Lewis J Rosa,José C Valentini,Sandro R Cicarelli,Regina MB |
author_role |
author |
author2 |
Ambrósio,Daniela L Trevelin,Caroline C Watanabe,Tatiana F Laure,Helen J Greene,Lewis J Rosa,José C Valentini,Sandro R Cicarelli,Regina MB |
author2_role |
author author author author author author author author |
dc.contributor.author.fl_str_mv |
Silva,Marco Túlio A da Ambrósio,Daniela L Trevelin,Caroline C Watanabe,Tatiana F Laure,Helen J Greene,Lewis J Rosa,José C Valentini,Sandro R Cicarelli,Regina MB |
dc.subject.por.fl_str_mv |
trans splicing cis splicing U5 snRNP U5-Cwc-21 PTP-Tag Trypanosoma cruzi Trypanosoma brucei |
topic |
trans splicing cis splicing U5 snRNP U5-Cwc-21 PTP-Tag Trypanosoma cruzi Trypanosoma brucei |
dc.description.none.fl_txt_mv |
Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes. In this context, certain small complexes of RNA and protein, which are named small nuclear ribonucleoproteins (U snRNPs), have an essential role in pre-mRNA processing, mainly during splicing. Even though they are well defined in mammals, snRNPs are still not well characterized in trypanosomatids. This study shows that a U5-15K protein is highly conserved among various trypanosomatid species. Tandem affinity pull-down assays revealed that this protein interacts with a novel U5-102K protein, which suggests the presence of a sub-complex that is potentially involved in the assembly of U4/U6-U5 tri-snRNPs. Functional analyses showed that U5-15K is essential for cell viability and is somehow involved with the trans and cis splicing machinery. Similar tandem affinity experiments with a trypanonosomatid U5-Cwc21 protein led to the purification of four U5 snRNP specific proteins and a Sm core, suggesting U5-Cwc-21 participation in the 35S U5 snRNP particle. Of these proteins, U5-200K was molecularly characterized. U5-200K has conserved domains, such as the DEAD/DEAH box helicase and Sec63 domains and displays a strong interaction with U5 snRNA. |
description |
Several protozoan parasites exist in the Trypanosomatidae family, including various agents of human diseases. Multiple lines of evidence suggest that important differences are present between the translational and mRNA processing (trans splicing) systems of trypanosomatids and other eukaryotes. In this context, certain small complexes of RNA and protein, which are named small nuclear ribonucleoproteins (U snRNPs), have an essential role in pre-mRNA processing, mainly during splicing. Even though they are well defined in mammals, snRNPs are still not well characterized in trypanosomatids. This study shows that a U5-15K protein is highly conserved among various trypanosomatid species. Tandem affinity pull-down assays revealed that this protein interacts with a novel U5-102K protein, which suggests the presence of a sub-complex that is potentially involved in the assembly of U4/U6-U5 tri-snRNPs. Functional analyses showed that U5-15K is essential for cell viability and is somehow involved with the trans and cis splicing machinery. Similar tandem affinity experiments with a trypanonosomatid U5-Cwc21 protein led to the purification of four U5 snRNP specific proteins and a Sm core, suggesting U5-Cwc-21 participation in the 35S U5 snRNP particle. Of these proteins, U5-200K was molecularly characterized. U5-200K has conserved domains, such as the DEAD/DEAH box helicase and Sec63 domains and displays a strong interaction with U5 snRNA. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-03-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200003 |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000200003 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0074-02762011000200003 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
publisher.none.fl_str_mv |
Instituto Oswaldo Cruz, Ministério da Saúde |
dc.source.none.fl_str_mv |
Memórias do Instituto Oswaldo Cruz v.106 n.2 2011 reponame:Memórias do Instituto Oswaldo Cruz instname:Fundação Oswaldo Cruz instacron:FIOCRUZ |
reponame_str |
Memórias do Instituto Oswaldo Cruz |
collection |
Memórias do Instituto Oswaldo Cruz |
instname_str |
Fundação Oswaldo Cruz |
instacron_str |
FIOCRUZ |
institution |
FIOCRUZ |
repository.name.fl_str_mv |
Memórias do Instituto Oswaldo Cruz - Fundação Oswaldo Cruz |
repository.mail.fl_str_mv |
|
_version_ |
1669937708892422144 |