Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Beata, Kmiec"'
Publikováno v:
Journal of experimental botany. 73(1)
Plant endosymbiotic organelles such as mitochondria and chloroplasts harbour a wide array of biochemical reactions. As a part of protein homeostasis to maintain organellar activity and stability, unwanted proteins and peptides need to be completely d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::676e60769e4f45203447b789ef390b2d
https://pubmed.ncbi.nlm.nih.gov/34460901
https://pubmed.ncbi.nlm.nih.gov/34460901
Autor:
Shaobai Huang, James Whelan, Pedro Teixeira, Rui M. M. Branca, Beata Kmiec, Aneta Ivanova, Monika W. Murcha, Mabel Gill-Hille, Janne Lehtiö
Publikováno v:
Plant Physiology. 181:1632-1650
Complex I biogenesis requires the expression of both nuclear and mitochondrial genes, the import of proteins, cofactor biosynthesis, and the assembly of at least 49 individual subunits. Assembly factors interact with subunits of Complex I but are not
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c5d20f7aef228907da9f40082198c0c8
https://doi.org/10.1104/pp.19.00822
https://doi.org/10.1104/pp.19.00822
Autor:
Pedro Teixeira, Beata Kmiec, Abi S Ghifari, Elzbieta Glaser, Adriana Pružinská, Monika W. Murcha
Publikováno v:
The Plant journal : for cell and molecular biologyREFERENCES. 104(5)
Most mitochondrial proteins are synthesised in the cytosol and targeted into the organelle via N-terminal targeting peptides that are cleaved upon import. The free targeting peptide is subsequently processed in a stepwise manner, with single amino ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1cb947a09df35e9a8d5ab87964a5362
https://pubmed.ncbi.nlm.nih.gov/32920905
https://pubmed.ncbi.nlm.nih.gov/32920905
Autor:
Rui M. M. Branca, Elzbieta Glaser, Beata Kmiec, Pedro Teixeira, Janne Lehtiö, Monika W. Murcha
Publikováno v:
Molecular Plant. 11:342-345
A Common Peptidolytic Mechanism for Targeting Peptide Degradation in Mitochondria and Chloroplasts
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::435af9666aa833cf40dba346ea19c64d
https://doi.org/10.1016/j.molp.2017.11.008
https://doi.org/10.1016/j.molp.2017.11.008
Autor:
Ronnie P.-A. Berntsson, Cecilia Wallin, Beata Kmiec, Pål Stenmark, Maria Ankarcrona, Geoffrey Masuyer, Sebastian K.T.S. Wärmländer, Pedro Teixeira, Astrid Gräslund, Janne Lehtiö, Rui M. M. Branca, Catarina Moreira Pinho, Elzbieta Glaser
Publikováno v:
Journal of Molecular Biology. 430:348-362
Proteolysis plays an important role in mitochondrial biogenesis, from the processing of newly imported precursor proteins to the degradation of mitochondrial targeting peptides. Disruption of peptide degradation activity in yeast, plant and mammalian
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f5eaa16a6f7cf6135de395f1aa8b33d
https://doi.org/10.1016/j.jmb.2017.11.011
https://doi.org/10.1016/j.jmb.2017.11.011
Autor:
Ute Roessner, Yan Wang, Chris Carrie, Shaobai Huang, James Whelan, Beata Kmiec, Owen Duncan, Monika W. Murcha, Pedro Teixeira, Oliver Berkowitz, Elzbieta Glaser, Simon R. Law, Wenhui Lyu, A. Harvey Millar, Jordan D. Radomiljac, Reena Narsai, Olivier Van Aken
Publikováno v:
Molecular Plant. 9:696-710
At12Cys-1 (At5g64400) and At12Cys-2 (At5g09570) are two closely related isogenes that encode small, twin cysteine proteins, typically located in mitochondria. At12Cys-2 transcript is induced in a variety of mutants with disrupted mitochondrial protei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42efee7eb1a77b0289de32f66900ff25
https://doi.org/10.1016/j.molp.2016.01.009
https://doi.org/10.1016/j.molp.2016.01.009
Autor:
Beata Kmiec, Lu Li, Rui M. M. Branca, Elzbieta Glaser, Yan Wang, James Whelan, Oliver Berkowitz, Janne Lehtiö, Pedro Teixeira, Monika W. Murcha
Publikováno v:
The Plant journal : for cell and molecular biology. 96(4)
The stepwise degradation of peptides to amino acids in plant mitochondria and chloroplasts is catalyzed by a network of oligopeptidases (presequence protease PreP, organellar oligopeptidase OOP) and aminopeptidases. In the present report, we show tha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5a4f603aa66e5f2d72d34167a3eea132
https://pubmed.ncbi.nlm.nih.gov/30422378
https://pubmed.ncbi.nlm.nih.gov/30422378
Publikováno v:
Trends in Plant Science. 19:771-778
The biogenesis and functionality of mitochondria and chloroplasts depend on the constant turnover of their proteins. The majority of mitochondrial and chloroplastic proteins are imported as precursors via their N-terminal targeting peptides. After im
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d66e236800b76ba36a65d2bd3d70950d
https://doi.org/10.1016/j.tplants.2014.09.004
https://doi.org/10.1016/j.tplants.2014.09.004
Autor:
Aneta Ivanova, Pedro Teixeira, Janne Lehtiö, Anna Byzia, Marcin Drag, Rui M. M. Branca, Beata Kmiec, Elzbieta Glaser, James Whelan, Monika W. Murcha
Publikováno v:
Nature Chemical Biology. 13:15-17
Plastids (including chloroplasts) are subcellular sites for a plethora of proteolytic reactions, required in functions ranging from protein biogenesis to quality control. Here we show that peptides generated from pre-protein maturation within chlorop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::81a15727ca8f695c211223a24c6f27cf
https://doi.org/10.1038/nchembio.2227
https://doi.org/10.1038/nchembio.2227
Autor:
James Whelan, Pedro Teixeira, Beata Kmiec, Monika W. Murcha, Szymon Kubiszewski-Jakubiak, Elzbieta Glaser
Publikováno v:
Journal of Experimental Botany. 65:6301-6335
The majority of more than 1000 proteins present in mitochondria are imported from nuclear-encoded, cytosolically synthesized precursor proteins. This impressive feat of transport and sorting is achieved by the combined action of targeting signals on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e2f5b58af19fd9fab36916fdafdff76a
https://doi.org/10.1093/jxb/eru399
https://doi.org/10.1093/jxb/eru399