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36 results on '"Khrouchtchova, Anastassia"'

4. SVR4 (suppressor of variegation 4) and SVR4-like:two proteins with a role in proper organization of the chloroplast genetic machinery

Author

Powikrowska, Marta, Khrouchtchova, Anastassia, Martens, Helle Juel, Nielsen, Agnieszka Janina Zygadlo, Melonek, Jonna, Schulz, Alexander, Krupinska, Karin, Rodermel, Steven, Jensen, Poul Erik, Powikrowska, Marta, Khrouchtchova, Anastassia, Martens, Helle Juel, Nielsen, Agnieszka Janina Zygadlo, Melonek, Jonna, Schulz, Alexander, Krupinska, Karin, Rodermel, Steven, and Jensen, Poul Erik

Published
2014

10. AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II

Author

Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Fristedt, Rikard, Vener, Alexander V., Scheller, Henrik Vibe, Jensen, Poul Erik, Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Fristedt, Rikard, Vener, Alexander V., Scheller, Henrik Vibe, Jensen, Poul Erik, Aro, Eva-Mari, and Haldrup, Anna

Published
2008

15. Thylakoid lumen immunophilin TLP40 is crucial for proper PSII assembly and a prerequisite for plant survival in short photoperiod

Author

Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Vener, Alexander, Scheller, Henrik Vibe, Jensen, Poul Erik, Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Vener, Alexander, Scheller, Henrik Vibe, Jensen, Poul Erik, Aro, Eva-Mari, and Haldrup, Anna

Published
2007

17. An immunophillin in the thylakoid lumen is potentially involved in assembly of PSII

Author

Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Fristedt, Rikard, Vener, Alexander, Aro, Eva-Mari, Jensen, Poul Erik, Scheller, Henrik Vibe, Haldrup, Anna, Khrouchtchova, Anastassia, Sirpiö, Sari, Allahverdiyeva, Yagut, Hansson, Maria, Fristedt, Rikard, Vener, Alexander, Aro, Eva-Mari, Jensen, Poul Erik, Scheller, Henrik Vibe, and Haldrup, Anna

Published
2007

18. Productivity:thylakoid lumenal protein TLP40 is crucial for plant survival af short day periods

Author

Khrouchtchova, Anastassia, Kristiansen, Kim Anker, Stenbæk, Anne, Hansson, Andreas, Edvardsson, Anna, Sirpiö, Sari, Paakkarinen, Virpi, Hansson, Maria, Vener, Alexander, Aro, Eva-Mari, Schulz, Alexander, Jensen, Poul Erik, Haldrup, Anna, Scheller, Henrik Vibe, Khrouchtchova, Anastassia, Kristiansen, Kim Anker, Stenbæk, Anne, Hansson, Andreas, Edvardsson, Anna, Sirpiö, Sari, Paakkarinen, Virpi, Hansson, Maria, Vener, Alexander, Aro, Eva-Mari, Schulz, Alexander, Jensen, Poul Erik, Haldrup, Anna, and Scheller, Henrik Vibe

Published
2007

19. An immunophilin in the thylakoid lumen is potentially involved in assembly of light harvesting proteins

Author

Khrouchtchova, Anastassia, Stenbæk, Anne, Hansson, Andreas, Edvardsson, Anna, Sirpiö, Sari, Paakkarinen, Virpi, Hansson, Maria, Vene,, Alexander, Aro, Eva-Mari, Jensen, Poul Erik, Scheller, Henrik Vibe, Haldrup, Anna, Khrouchtchova, Anastassia, Stenbæk, Anne, Hansson, Andreas, Edvardsson, Anna, Sirpiö, Sari, Paakkarinen, Virpi, Hansson, Maria, Vene,, Alexander, Aro, Eva-Mari, Jensen, Poul Erik, Scheller, Henrik Vibe, and Haldrup, Anna

Published
2007

20. A previously found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of plant photosystem I and is designated PSI-P

Author

Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Alexander V., Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Alexander V., Aro, Eva-Mari, and Haldrup, Anna

Published
2006

22. PSI-P - a new subunit of plant photosystem I

Author

Khrouchtchova, Anastassia, Paakkarinen, Virpi, Vainonen, Julia P., Hansson, Maria, Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Aleander V., Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Paakkarinen, Virpi, Vainonen, Julia P., Hansson, Maria, Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Aleander V., Aro, Eva-Mari, and Haldrup, Anna

Published
2006

23. A previosly found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of photosystem I and is designated PSI-P

Author

Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Vibe Scheller, Henrik, Vener, Alexander V., Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Vibe Scheller, Henrik, Vener, Alexander V., Aro, Eva-Mari, and Haldrup, Anna

Abstract

We show that the thylakoid membrane phosphoprotein TMP14 is a novel subunit of plant photosystem I (PSI). Blue native/SDS–PAGE and sucrose gradient fractionation demonstrated the association of the protein exclusively with PSI. We designate the protein PSI-P. The presence of PSI-P subunit in Arabidopsis mutants lacking other PSI subunits was analyzed and suggested a location in the proximity of PSI-L, -H and -O subunits. The PSI-P protein was not differentially phosphorylated in state 1 and state 2.

Published
2005
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24. PSI-P - a new subunit of plant photosystem I

Author

Khrouchtchova, Anastassia, Paakkarinen, V., Vainonen, J., Hansson, M, Zhang, Zuping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, A., Aro, E.M., Haldrup, Anna, Khrouchtchova, Anastassia, Paakkarinen, V., Vainonen, J., Hansson, M, Zhang, Zuping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, A., Aro, E.M., and Haldrup, Anna

Published
2005

27. A previously found thylakoid membrane protein of 14 kDa (TMP14) is a novel subunit of plant photosystem I and is designed PSI-P

Author

Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Alexander V., Aro, Eva-Mari, Haldrup, Anna, Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Alexander V., Aro, Eva-Mari, and Haldrup, Anna

Published
2005

33. SVR4 (suppressor of variegation 4) and SVR4-like: two proteins with a role in proper organization of the chloroplast genetic machinery.

Author

Powikrowska, Marta, Khrouchtchova, Anastassia, Martens, Helle Juel, Zygadlo‐Nielsen, Agnieszka, Melonek, Joanna, Schulz, Alexander, Krupinska, Karin, Rodermel, Steven, and Jensen, Poul Erik

Subjects
*VARIEGATION, *CHLOROPLASTS, *MUTANT proteins, *PHOTOSYNTHETIC pigments, *GENE expression, *GENE regulatory networks
Abstract

SUPPRESSOR OF VARIEGATION 4 (SVR4, also called MRL7) and its homolog SVR4-like (also called MRL7-Like) were originally identified as important proteins for proper function of the chloroplast in Arabidopsis. Both are nuclear-encoded chloroplast-located proteins, and knockout mutants of either gene result in seedling lethality. Transmission electron microscopy analysis revealed that chloroplast development is arrested at an early developmental stage in both mutants. Accordingly, in the mutant plants severely decreased levels of photosynthetic pigments as well as subunits of the photosynthetic complexes could be detected. In absence of either of the two proteins chloroplast DNA organization was clearly affected. Immunological analysis revealed that SVR4 is a component of the transcriptionally active chromosome (TAC) from barley chloroplasts. Analyses of gene expression indicate that SVR4 and SVR4-like are required for proper function of the plastid transcriptional machinery. We propose that SVR4 and SVR4-like function as molecular chaperones ensuring proper organization of the nucleoids in chloroplasts. [ABSTRACT FROM AUTHOR]

Published
2014
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34. SUPPRESSOR OF VARIEGATION4, a New var2 Suppressor Locus, Encodes a Pioneer Protein that Is Required for Chloroplast Biogenesis.

Author

Fei Yua, Sung-Soon Park, Xiayan Liu, Foudree, Andrew, Aigen Fu, Powikrowska, Marta, Khrouchtchova, Anastassia, Jensen, Poul Erik, Kriger, Jillian N., Gray, Gordon R., and Rodermel, Steven R.

Subjects
CHLOROPLAST formation, ORGANELLES, ARABIDOPSIS, METALLOPROTEINASES, VARIEGATED plants
Abstract

VAR2 is an integral thylakoid membrane protein and a member of the versatile FtsH class of metalloproteases in prokaryotes and eukaryotes. Recessive mutations in the VAR2 locus give rise to variegated plants (var2) that contain white sectors with abnormal plastids and green sectors with normal-appearing chloroplasts. In a continuing effort to isolate second-site suppressors of var2 variegation, we characterize in this report ems2505, a suppressor strain that has a virescent phenotype due to a missense mutation in At4g28590, the gene for a pioneer protein. We designated this gene SVR4 (for SUPPRESSOR OF VARIEGATION4) and the mutant allele in ems2505 as svr4-1. We demonstrate that SVR4 is located in chloroplasts and that svr4-1 single mutants are normal with respect to chloroplast anatomy and thylakoid membrane protein accumulation. However, they are modestly impaired in several aspects of photochemistry and have enhanced non-photochemical quenching (NPQ) capacity. A T-DNA insertion allele of SVR4, svr4-2, is seedling-lethal due to an early blockage of chloroplast development. We conclude that SVR4 is essential for chloroplast biogenesis, and hypothesize that SVR4 mediates some aspect of thylakoid structure or function that controls NPQ. We propose that in the suppressor strain, photoinhibitory pressure caused by a lack of VAR2 is ameliorated early in chloroplast development by enhanced NPQ capacity caused by reduced SVR4 activity. This would result in an increase in the number of chloroplasts that are able to surmount a threshold necessary to avoid photo-damage and thereby develop into functional chloroplasts. [ABSTRACT FROM PUBLISHER]

Published
2011
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35. AtCYP38 ensures early biogenesis, correct assembly and sustenance of photosystem II.

Author

Sirpi, Sari, Khrouchtchova, Anastassia, Allahverdiyeva, Yagut, Hansson, Maria, Fristedt, Rikard, Vener, Alexander V., Scheller, Henrik Vibe, Jensen, Poul Erik, Haldrup, Anna, and Aro, Eva-Mari

Subjects
*THYLAKOIDS, *PHOSPHATASES, *PHOSPHORYLATION, *CHEMICAL reactions, *PROTEINS, *ESTERASES
Abstract

AtCYP38 is a thylakoid lumen protein comprising the immunophilin domain and the phosphatase inhibitor module. Here we show the association of AtCYP38 with the photosystem II (PSII) monomer complex and address its functional role using AtCYP38-deficient mutants. The dynamic greening process of etiolated leaves failed in the absence of AtCYP38, due to specific problems in the biogenesis of PSII complexes. Also the development of leaves under short-day conditions was severely disturbed. Detailed biophysical and biochemical analysis of mature AtCYP38-deficient plants from favorable growth conditions (long photoperiod) revealed: (i) intrinsic malfunction of PSII, which (ii) occurred on the donor side of PSII and (iii) was dependent on growing light intensity. AtCYP38 mutant plants also showed decreased accumulation of PSII, which was shown not to originate from impaired D1 synthesis or assembly of PSII monomers, dimers and supercomplexes as such but rather from the incorrect fine-tuning of the oxygen-evolving side of PSII. This, in turn, rendered PSII centers extremely susceptible to photoinhibition. AtCYP38 deficiency also drastically decreased the in vivo phosphorylation of PSII core proteins, probably related to the absence of the AtCYP38 phosphatase inhibitor domain. It is proposed that during PSII assembly AtCYP38 protein guides the proper folding of D1 (and CP43) into PSII, thereby enabling the correct assembly of the water-splitting Mn4–Ca cluster even with high turnover of PSII. [ABSTRACT FROM AUTHOR]

Published
2008
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36. A previously found thylakoid membrane protein of 14kDa (TMP14) is a novel subunit of plant photosystem I and is designated PSI-P

Author

Khrouchtchova, Anastassia, Hansson, Maria, Paakkarinen, Virpi, Vainonen, Julia P., Zhang, Suping, Jensen, Poul Erik, Scheller, Henrik Vibe, Vener, Alexander V., Aro, Eva-Mari, and Haldrup, Anna

Subjects
*THYLAKOIDS, *ARABIDOPSIS, *MEMBRANE proteins, *SUCROSE
Abstract

Abstract: We show that the thylakoid membrane phosphoprotein TMP14 is a novel subunit of plant photosystem I (PSI). Blue native/SDS–PAGE and sucrose gradient fractionation demonstrated the association of the protein exclusively with PSI. We designate the protein PSI-P. The presence of PSI-P subunit in Arabidopsis mutants lacking other PSI subunits was analyzed and suggested a location in the proximity of PSI-L, -H and -O subunits. The PSI-P protein was not differentially phosphorylated in state 1 and state 2. [Copyright &y& Elsevier]

Published
2005
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