Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation
P in1‐type peptidyl‐prolyl cis/trans isomerases ( PPI ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a P in1‐type PPI ase in T rypanosoma cruzi , but little is known about its function and subcellular lo...
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| Veröffentlicht in: | The Journal of eukaryotic microbiology 2013-01, Vol.60 (1), p.101-105 |
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| container_title | The Journal of eukaryotic microbiology |
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| creator | Erben, Esteban D. Nardelli, Sheila C. de Jesus, Teresa C. L. Schenkman, Sergio Tellez‐Iñon, Maria T. |
| description | P
in1‐type peptidyl‐prolyl
cis/trans
isomerases (
PPI
ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a
P
in1‐type
PPI
ase in
T
rypanosoma cruzi
, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with
P
in1‐like proteins from diverse organisms,
Tc
P
in1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition,
RNAi
‐mediated downregulation of
Tb
P
in1 in
T
rypanosoma brucei
did not abolish cell proliferation. Using yeast two‐hybrid assay, we identified a
MORN
domain‐containing protein as putative
P
in1‐binding partners. These data suggest that
P
in1‐mediated signaling mechanism plays a different role in protozoan parasites. |
| doi_str_mv | 10.1111/jeu.12009 |
| format | Article |
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in1‐type peptidyl‐prolyl
cis/trans
isomerases (
PPI
ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a
P
in1‐type
PPI
ase in
T
rypanosoma cruzi
, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with
P
in1‐like proteins from diverse organisms,
Tc
P
in1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition,
RNAi
‐mediated downregulation of
Tb
P
in1 in
T
rypanosoma brucei
did not abolish cell proliferation. Using yeast two‐hybrid assay, we identified a
MORN
domain‐containing protein as putative
P
in1‐binding partners. These data suggest that
P
in1‐mediated signaling mechanism plays a different role in protozoan parasites.</description><identifier>ISSN: 1066-5234</identifier><identifier>EISSN: 1550-7408</identifier><identifier>DOI: 10.1111/jeu.12009</identifier><language>eng</language><ispartof>The Journal of eukaryotic microbiology, 2013-01, Vol.60 (1), p.101-105</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c749-bf05ec3b6271187acb436513ea6519e8016e1b0de4b6f9b2ca157ece5e5829ef3</citedby><cites>FETCH-LOGICAL-c749-bf05ec3b6271187acb436513ea6519e8016e1b0de4b6f9b2ca157ece5e5829ef3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids></links><search><creatorcontrib>Erben, Esteban D.</creatorcontrib><creatorcontrib>Nardelli, Sheila C.</creatorcontrib><creatorcontrib>de Jesus, Teresa C. L.</creatorcontrib><creatorcontrib>Schenkman, Sergio</creatorcontrib><creatorcontrib>Tellez‐Iñon, Maria T.</creatorcontrib><title>Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation</title><title>The Journal of eukaryotic microbiology</title><description>P
in1‐type peptidyl‐prolyl
cis/trans
isomerases (
PPI
ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a
P
in1‐type
PPI
ase in
T
rypanosoma cruzi
, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with
P
in1‐like proteins from diverse organisms,
Tc
P
in1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition,
RNAi
‐mediated downregulation of
Tb
P
in1 in
T
rypanosoma brucei
did not abolish cell proliferation. Using yeast two‐hybrid assay, we identified a
MORN
domain‐containing protein as putative
P
in1‐binding partners. These data suggest that
P
in1‐mediated signaling mechanism plays a different role in protozoan parasites.</description><issn>1066-5234</issn><issn>1550-7408</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><recordid>eNotkL9OxDAMxiMEEsfBwBtkZegRt03_jKg64KQTdOhepakj5ZQ2VVKGbDwCz8iTkAM82J8t_yzrI-Qe2A5iPJ7wYwcpY_UF2QDnLClzVl1GzYoi4WmWX5Mb70-MQZECbMjUubCI2Xo7iVWPtKV6hu_Pry4sSFtc4iyY2LfOmmDoIe6hEx6jok1YI2e0pGIe6Ztd6d57nFctDFXW0QaNoWdQq8is2s635EoJ4_Huv25J97zvmtfk-P5yaJ6OiSzzOhkU4yizoUhLgKoUcsizgkOGIuYaq_g7wsBGzIdC1UMqBfASJXLkVVqjyrbk4e-sdNZ7h6pfnJ6ECz2w_mxTH23qf23KfgAgvF5-</recordid><startdate>201301</startdate><enddate>201301</enddate><creator>Erben, Esteban D.</creator><creator>Nardelli, Sheila C.</creator><creator>de Jesus, Teresa C. L.</creator><creator>Schenkman, Sergio</creator><creator>Tellez‐Iñon, Maria T.</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>201301</creationdate><title>Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation</title><author>Erben, Esteban D. ; Nardelli, Sheila C. ; de Jesus, Teresa C. L. ; Schenkman, Sergio ; Tellez‐Iñon, Maria T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c749-bf05ec3b6271187acb436513ea6519e8016e1b0de4b6f9b2ca157ece5e5829ef3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Erben, Esteban D.</creatorcontrib><creatorcontrib>Nardelli, Sheila C.</creatorcontrib><creatorcontrib>de Jesus, Teresa C. L.</creatorcontrib><creatorcontrib>Schenkman, Sergio</creatorcontrib><creatorcontrib>Tellez‐Iñon, Maria T.</creatorcontrib><collection>CrossRef</collection><jtitle>The Journal of eukaryotic microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Erben, Esteban D.</au><au>Nardelli, Sheila C.</au><au>de Jesus, Teresa C. L.</au><au>Schenkman, Sergio</au><au>Tellez‐Iñon, Maria T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation</atitle><jtitle>The Journal of eukaryotic microbiology</jtitle><date>2013-01</date><risdate>2013</risdate><volume>60</volume><issue>1</issue><spage>101</spage><epage>105</epage><pages>101-105</pages><issn>1066-5234</issn><eissn>1550-7408</eissn><abstract>P
in1‐type peptidyl‐prolyl
cis/trans
isomerases (
PPI
ases) isomerise the peptide bond of specific phosphorylated (Ser/Thr)‐Pro residues, regulating various cellular events. Previously, we reported a
P
in1‐type
PPI
ase in
T
rypanosoma cruzi
, but little is known about its function and subcellular localization. Immunofluorescence analysis revealed that in contrast with
P
in1‐like proteins from diverse organisms,
Tc
P
in1 mainly localized in the cytoplasm and was excluded from the nuclei. In addition,
RNAi
‐mediated downregulation of
Tb
P
in1 in
T
rypanosoma brucei
did not abolish cell proliferation. Using yeast two‐hybrid assay, we identified a
MORN
domain‐containing protein as putative
P
in1‐binding partners. These data suggest that
P
in1‐mediated signaling mechanism plays a different role in protozoan parasites.</abstract><doi>10.1111/jeu.12009</doi><tpages>5</tpages></addata></record> |
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| ispartof | The Journal of eukaryotic microbiology, 2013-01, Vol.60 (1), p.101-105 |
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| language | eng |
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| source | Wiley Online Library Journals Frontfile Complete |
| title | Trypanosomatid P in1‐Type Peptidyl‐Prolyl Isomerase Is Cytosolic and Not Essential for Cell Proliferation |
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