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المؤلفون: Vorphal, María, Bruna, Carola, Traudy Wandersleben, Dagnino-Leone, Jorge, Lobos-González, Francisco, Uribe, Elena, Martínez-Oyanedel, José, Bunster, Marta
الوصف: Additional file 3. Specific information regarding the determination of the sequence and cloning of FNR from Gracilaria chilensis.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::293d901d92ff2dfab01d87a7ccf66effTest
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المؤلفون: Vorphal, María, Bruna, Carola, Traudy Wandersleben, Dagnino-Leone, Jorge, Lobos-González, Francisco, Uribe, Elena, Martínez-Oyanedel, José, Bunster, Marta
الوصف: Additional file 2. Spectroscopic characterization of purified phycobilisomes.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::511a3e71c1e985a1c997a6f5a12ab9e4Test
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المؤلفون: Vorphal, María, Bruna, Carola, Traudy Wandersleben, Dagnino-Leone, Jorge, Lobos-González, Francisco, Uribe, Elena, Martínez-Oyanedel, José, Bunster, Marta
الوصف: Additional file 1. PBS purification protocol.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7bedd46f0d92967c0297673ce4ac2fa0Test
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المؤلفون: Vorphal, María, Bruna, Carola, Traudy Wandersleben, Dagnino-Leone, Jorge, Lobos-González, Francisco, Uribe, Elena, Martínez-Oyanedel, José, Bunster, Marta
الوصف: Additional file 4. Saturation curve and Lineweaver-Burk plot for the enzymatic activity of FNR present in PBS of Gracilaria chilensis.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2b1529b36eb9b6cb610f20060c4919bTest
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المصدر: Latin american journal of aquatic research, Volume: 43, Issue: 4, Pages: 798-806, Published: SEP 2015
مصطلحات موضوعية: reproduction, diatomeas, blooms, copepods, florecimientos masivos, food, copépodos, perfiles de proteínas, protein profiles, alimento, diatoms, reproducción
الوصف: Recent field and experimental evidence collected in the southern upwelling region off Concepción (36°5'S, 73°3'W) showed an abrupt reduction (
وصف الملف: text/html
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=od_______614::0210df45bde8c211d530ca649ecc732cTest
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0718-560X2015000400020&lng=en&tlng=enTest -
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المؤلفون: Vásquez-Suárez, Aleikar, Lobos-González, Francisco, Cronshaw, Andrew, Sepúlveda-Ugarte, José, Figueroa, Maximiliano, Dagnino-Leone, Jorge, Bunster, Marta, Martínez-Oyanedel, José
المصدر: PLoS ONE, Vol 13, Iss 7, p e0200867 (2018)
PLoS ONEمصطلحات موضوعية: Multidisciplinary, lcsh:R, Correction, lcsh:Medicine, Phycoerythrin, Protein Subunits, Phycobilins, Gracilaria, lcsh:Q, Amino Acid Sequence, Urobilin, lcsh:Science, Sequence Analysis, Plant Proteins
الوصف: Phycobilisomes (PBS) are accessory light harvesting protein complexes formed mainly by phycobiliproteins (PBPs). The PBPs absorb light that is efficiently transferred to Photosystems due to chromophores covalently bound to specific cysteine residues. Besides phycobiliproteins (PE), the PBS contains linker proteins responsible for assembly and stabilization of the whole complex and the tuning of energy transfer steps between chromophores. The linker (γ33) from Gracilaria chilensis, is a chromophorylated rod linker associated to (αβ)6 hexamers of R-phycoerythrin (R-PE). Its role in the energy transfer process is not clear yet. Structural studies as well as the composition and location of the chromophores are essential to understand their involvement in the energy transfer process in PBS. To achieve this, the coding gene of γ33 was cloned and sequenced. The sequence was analyzed by informatics tools, to obtain preliminary information which leaded the next experiments. The protein was purified from R-phycoerythrin, and the sequence confirmed by mass spectrometry. The coding sequence analysis revealed a protein of 318 aminoacid residues containing a chloroplastidial transit peptide (cTP) of 39 aminoacids at the N-terminus. The conservation of cysteines revealed possible chromophorylation sites. Using α and β R-PE subunits as spectroscopic probes in denaturation assays, we deduced a double bonded phycourobilin (PUB) on γ33 subunit that were confirmed between Cys62 and Cys73 (DL-PUB62/73) by mass spectrometry. The cysteines involved in the double link are located in a helical region, in a conformation that reminds the position of the DL-PUB50/61 in the β subunit of R-PE. The position of single linked PUB at Cys95 and a single linked PEB at Cys172 were also confirmed. Spectroscopic studies show the presence of both types of chromophores and that there are not energy transfer by FRET among them.
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02c88510ec10e71eee76058364326f5fTest
https://doi.org/10.1371/journal.pone.0200867Test