Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Galetskiy, Dmitry; Susnea, Iuliana; Reiser, Verena; Adamska, Iwona; Przybylski, Michael

doi:10.1016/j.jasms.2008.03.014

Cited by 22 publications

(14 citation statements)

References 49 publications

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“…In contrast, the 25-kD acetylated protein band consisted of three neighboring spots, identified as LHCb1 and LHCb2 by LC/MS. The surrounding small spots were other LHCb minor isoforms, consistent with the report of Galetskiy et al (2008).…”

Section: Abundant Lysac Of Nonhistone Proteins In Arabidopsissupporting

confidence: 89%

Lysine Acetylation Is a Widespread Protein Modification for Diverse Proteins in Arabidopsis

et al. 2011

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Lysine acetylation (LysAc), a form of reversible protein posttranslational modification previously known only for histone regulation in plants, is shown to be widespread in Arabidopsis (Arabidopsis thaliana). Sixty-four Lys modification sites were identified on 57 proteins, which operate in a wide variety of pathways/processes and are located in various cellular compartments. A number of photosynthesis-related proteins are among this group of LysAc proteins, including photosystem II (PSII) subunits, light-harvesting chlorophyll a/b-binding proteins (LHCb), Rubisco large and small subunits, and chloroplastic ATP synthase (b-subunit). Using two-dimensional native green/sodium dodecyl sulfate gels, the loosely PSII-bound LHCb was separated from the LHCb that is tightly bound to PSII and shown to have substantially higher level of LysAc, implying that LysAc may play a role in distributing the LHCb complexes. Several potential LysAc sites were identified on eukaryotic elongation factor-1A (eEF-1A) by liquid chromatography/mass spectrometry and using sequence-and modification-specific antibodies the acetylation of Lys-227 and Lys-306 was established. Lys-306 is contained within a predicted calmodulin-binding sequence and acetylation of Lys-306 strongly inhibited the interactions of eEF-1A synthetic peptides with calmodulin recombinant proteins in vitro. These results suggest that LysAc of eEF-1A may directly affect regulatory properties and localization of the protein within the cell. Overall, these findings reveal the possibility that reversible LysAc may be an important and previously unknown regulatory mechanism of a large number of nonhistone proteins affecting a wide range of pathways and processes in Arabidopsis and likely in all plants.

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Section: Abundant Lysac Of Nonhistone Proteins In Arabidopsissupporting

confidence: 89%

Lysine Acetylation Is a Widespread Protein Modification for Diverse Proteins in Arabidopsis

et al. 2011

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“…FIB4 is found associated with the PSII light-harvesting complex (Galetskiy et al, 2008). FIB4 has also been detected in plastoglobules Ytterberg et al, 2006) and thylakoids (Friso et al, 2004;Peltier et al, 2004).…”

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confidence: 97%

“…The Arabidopsis fibrillin encoded by At3g23400 has received various appellations, including FIBRILLIN4 (FIB4; Laizet et al, 2004), Harpin-Binding Protein1 (Song et al, 2002), AtPGL 30.4 , and Fibrillin6 (Galetskiy et al, 2008); here, it will be referred to by its earliest published name, FIB4. FIB4 is found associated with the PSII light-harvesting complex (Galetskiy et al, 2008).…”

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confidence: 99%

FIBRILLIN4Is Required for Plastoglobule Development and Stress Resistance in Apple and Arabidopsis

et al. 2010

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The fibrillins are a large family of chloroplast proteins that have been linked with stress tolerance and disease resistance. FIBRILLIN4 (FIB4) is found associated with the photosystem II light-harvesting complex, thylakoids, and plastoglobules, which are chloroplast compartments rich in lipophilic antioxidants. For this study, FIB4 expression was knocked down in apple (Malus 3 domestica) using RNA interference. Plastoglobule osmiophilicity was decreased in fib4 knockdown (fib4 KD) tree chloroplasts compared with the wild type, while total plastoglobule number was unchanged. Compared with the wild type, net photosynthetic CO 2 fixation in fib4 KD trees was decreased at high light intensity but was increased at low light intensity. Furthermore, fib4 KD trees produced more anthocyanins than the wild type when transferred from low to high light intensity, indicating greater sensitivity to high light stress. Relative to the wild type, fib4 KD apples were more sensitive to methyl viologen and had higher superoxide levels during methyl viologen treatment. Arabidopsis (Arabidopsis thaliana) fib4 mutants and fib4 KD apples were more susceptible than their wild-type counterparts to the bacterial pathogens Pseudomonas syringae pathovar tomato and Erwinia amylovora, respectively, and were more sensitive to ozone-induced tissue damage. Following ozone stress, plastoglobule osmiophilicity decreased in wild-type apple and remained low in fib4 KD trees; total plastoglobule number increased in fib4 KD apples but not in the wild type. These results indicate that FIB4 is required for plastoglobule development and resistance to multiple stresses. This study suggests that FIB4 is involved in regulating plastoglobule content and that defective regulation of plastoglobule content leads to broad stress sensitivity and altered photosynthetic activity.

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“…Silencing the four DIPM genes through genetic engineering also leads to a partial resistance to fire blight (11). Fibrillin (also known as FIBRILLIN4 and harpin-binding protein1) is associated with the photosystem II (PSII) light-harvesting complex (32) and physically interacts with the HrpN www.annualreviews.org • Fire Blight protein (110). Silencing the fib4 genes in apple increased the susceptibility of the transgenic lines compared with the control (101).…”

Section: Transgenic and Cisgenic Applicationsmentioning

confidence: 99%

Fire Blight: Applied Genomic Insights of the Pathogen and Host

Malnoy

Martens

Norelli

et al. 2012

Annu. Rev. Phytopathol.

130

101

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The enterobacterial phytopathogen Erwinia amylovora causes fire blight, an invasive disease that threatens a wide range of commercial and ornamental Rosaceae host plants. The response elicited by E. amylovora in its host during disease development is similar to the hypersensitive reaction that typically leads to resistance in an incompatible host-pathogen interaction, yet no gene-for-gene resistance has been described for this host-pathogen system. Comparative genomic analysis has found an unprecedented degree of genetic uniformity among strains of E. amylovora, suggesting that the pathogen has undergone a recent genetic bottleneck. The genome of apple, an important host of E. amylovora, has been sequenced, creating new opportunities for the study of interactions between host and pathogen during fire blight development and for the identification of resistance genes. This review includes recent advances in the genomics of both host and pathogen.

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Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Cited by 22 publications

References 49 publications

Lysine Acetylation Is a Widespread Protein Modification for Diverse Proteins in Arabidopsis

Lysine Acetylation Is a Widespread Protein Modification for Diverse Proteins in Arabidopsis

FIBRILLIN4Is Required for Plastoglobule Development and Stress Resistance in Apple and Arabidopsis

Fire Blight: Applied Genomic Insights of the Pathogen and Host

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