Plastoglobule-Targeting Competence of a Putative Transit Peptide Sequence from Rice Phytoene Synthase 2 in Plastids.
| Title: | Plastoglobule-Targeting Competence of a Putative Transit Peptide Sequence from Rice Phytoene Synthase 2 in Plastids. |
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| Authors: | Min Kyoung You, Jin Hwa Kim, Yeo Jin Lee, Ye Sol Jeong, Sun-Hwa Ha |
| Source: | International Journal of Molecular Sciences; Jan2017, Vol. 18 Issue 1, p18, 15p, 4 Diagrams, 2 Charts, 2 Graphs |
| Subject Terms: | THYLAKOIDS, AMINO acids, CHLOROPLASTS, PROTOPLASTS, MEMBRANE proteins |
| Abstract: | Plastoglobules (PGs) are thylakoid membrane microdomains within plastids that are known as specialized locations of carotenogenesis. Three rice phytoene synthase proteins (OsPSYs) involved in carotenoid biosynthesis have been identified. Here, the N-terminal 80-amino-acid portion of OsPSY2 (PTp) was demonstrated to be a chloroplast-targeting peptide by displaying cytosolic localization of OsPSY2(DPTp):mCherry in rice protoplast, in contrast to chloroplast localization of OsPSY2:mCherry in a punctate pattern. The peptide sequence of a PTp was predicted to harbor two transmembrane domains eligible for a putative PG-targeting signal. To assess and enhance the PG-targeting ability of PTp, the original PTp DNA sequence (PTp) was modified to a synthetic DNA sequence (stPTp), which had 84.4% similarity to the original sequence. The motivation of this modification was to reduce the GC ratio from 75% to 65% and to disentangle the hairpin loop structures of PTp. These two DNA sequences were fused to the sequence of the synthetic green fluorescent protein (sGFP) and drove GFP expression with different efficiencies. In particular, the RNA and protein levels of stPTp-sGFP were slightly improved to 1.4-fold and 1.3-fold more than those of sGFP, respectively. The green fluorescent signals of their mature proteins were all observed as speckle-like patterns with slightly blurred stromal signals in chloroplasts. These discrete green speckles of PTp-sGFP and stPTp-sGFP corresponded exactly to the red fluorescent signal displayed by OsPSY2:mCherry in both etiolated and greening protoplasts and it is presumed to correspond to distinct PGs. In conclusion, we identified PTp as a transit peptide sequence facilitating preferential translocation of foreign proteins to PGs, and developed an improved PTp sequence, a stPTp, which is expected to be very useful for applications in plant biotechnologies requiring precise micro-compartmental localization in plastids. [ABSTRACT FROM AUTHOR] |
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| Database: | Complementary Index |
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| Items | – Name: Title Label: Title Group: Ti Data: Plastoglobule-Targeting Competence of a Putative Transit Peptide Sequence from Rice Phytoene Synthase 2 in Plastids. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Min+Kyoung+You%22">Min Kyoung You</searchLink><br /><searchLink fieldCode="AR" term="%22Jin+Hwa+Kim%22">Jin Hwa Kim</searchLink><br /><searchLink fieldCode="AR" term="%22Yeo+Jin+Lee%22">Yeo Jin Lee</searchLink><br /><searchLink fieldCode="AR" term="%22Ye+Sol+Jeong%22">Ye Sol Jeong</searchLink><br /><searchLink fieldCode="AR" term="%22Sun-Hwa+Ha%22">Sun-Hwa Ha</searchLink> – Name: TitleSource Label: Source Group: Src Data: International Journal of Molecular Sciences; Jan2017, Vol. 18 Issue 1, p18, 15p, 4 Diagrams, 2 Charts, 2 Graphs – Name: Subject Label: Subject Terms Group: Su Data: <searchLink fieldCode="DE" term="%22THYLAKOIDS%22">THYLAKOIDS</searchLink><br /><searchLink fieldCode="DE" term="%22AMINO+acids%22">AMINO acids</searchLink><br /><searchLink fieldCode="DE" term="%22CHLOROPLASTS%22">CHLOROPLASTS</searchLink><br /><searchLink fieldCode="DE" term="%22PROTOPLASTS%22">PROTOPLASTS</searchLink><br /><searchLink fieldCode="DE" term="%22MEMBRANE+proteins%22">MEMBRANE proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Plastoglobules (PGs) are thylakoid membrane microdomains within plastids that are known as specialized locations of carotenogenesis. Three rice phytoene synthase proteins (OsPSYs) involved in carotenoid biosynthesis have been identified. Here, the N-terminal 80-amino-acid portion of OsPSY2 (PTp) was demonstrated to be a chloroplast-targeting peptide by displaying cytosolic localization of OsPSY2(DPTp):mCherry in rice protoplast, in contrast to chloroplast localization of OsPSY2:mCherry in a punctate pattern. The peptide sequence of a PTp was predicted to harbor two transmembrane domains eligible for a putative PG-targeting signal. To assess and enhance the PG-targeting ability of PTp, the original PTp DNA sequence (PTp) was modified to a synthetic DNA sequence (stPTp), which had 84.4% similarity to the original sequence. The motivation of this modification was to reduce the GC ratio from 75% to 65% and to disentangle the hairpin loop structures of PTp. These two DNA sequences were fused to the sequence of the synthetic green fluorescent protein (sGFP) and drove GFP expression with different efficiencies. In particular, the RNA and protein levels of stPTp-sGFP were slightly improved to 1.4-fold and 1.3-fold more than those of sGFP, respectively. The green fluorescent signals of their mature proteins were all observed as speckle-like patterns with slightly blurred stromal signals in chloroplasts. These discrete green speckles of PTp-sGFP and stPTp-sGFP corresponded exactly to the red fluorescent signal displayed by OsPSY2:mCherry in both etiolated and greening protoplasts and it is presumed to correspond to distinct PGs. In conclusion, we identified PTp as a transit peptide sequence facilitating preferential translocation of foreign proteins to PGs, and developed an improved PTp sequence, a stPTp, which is expected to be very useful for applications in plant biotechnologies requiring precise micro-compartmental localization in plastids. [ABSTRACT FROM AUTHOR] – Name: Abstract Label: Group: Ab Data: <i>Copyright of International Journal of Molecular Sciences is the property of MDPI and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.3390/ijms18010018 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 15 StartPage: 18 Subjects: – SubjectFull: THYLAKOIDS Type: general – SubjectFull: AMINO acids Type: general – SubjectFull: CHLOROPLASTS Type: general – SubjectFull: PROTOPLASTS Type: general – SubjectFull: MEMBRANE proteins Type: general Titles: – TitleFull: Plastoglobule-Targeting Competence of a Putative Transit Peptide Sequence from Rice Phytoene Synthase 2 in Plastids. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Min Kyoung You – PersonEntity: Name: NameFull: Jin Hwa Kim – PersonEntity: Name: NameFull: Yeo Jin Lee – PersonEntity: Name: NameFull: Ye Sol Jeong – PersonEntity: Name: NameFull: Sun-Hwa Ha IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 01 Text: Jan2017 Type: published Y: 2017 Identifiers: – Type: issn-print Value: 16616596 Numbering: – Type: volume Value: 18 – Type: issue Value: 1 Titles: – TitleFull: International Journal of Molecular Sciences Type: main |
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