Water-Soluble Chlorophyll Protein in Brassicaceae Plants is a Stress-Induced Chlorophyll-Binding Protein

2001 ◽  
Vol 42 (9) ◽  
pp. 906-911 ◽  
Author(s):  
Hiroyuki Satoh ◽  
Akira Uchida ◽  
Katsumi Nakayama ◽  
Mitsumasa Okada
Keyword(s):  
Binding Protein ◽  
Water Soluble ◽  
Chlorophyll Protein

Comparison between the human serum growth hormone-binding protein and the water-soluble growth hormone-binding site released from IM-9 lymphocytes

1993 ◽  
Vol 129 (6) ◽  
pp. 559-564 ◽  
Author(s):  
Guy Massa ◽  
Mapoko Ilondo ◽  
Magda Vanderschueren-Lodeweyckx
Keyword(s):  
Growth Hormone ◽  
Human Serum ◽  
Binding Site ◽  
Binding Protein ◽  
Water Soluble ◽  
Hormone Binding ◽  
Serum Growth Hormone ◽  
Gh Receptor ◽  
Growth Hormone Binding Protein ◽  
Hormone Binding Protein

The characteristics of the human serum growth hormone-binding protein (GHBP) were compared with those of a water-soluble GH-binding site prepared by incubating cultured IM-9 lymphocytes in assay buffer with 25 mmol/l iodoacetamide. High-performance liquid chromatography gel filtration of the water-soluble GH-binding site incubated with 125I-labeled human GH ([125I]hGH) revealed a large peak of bound [125I]hGH eluting at the same position as the peak of [125I]hGH bound to the GHBP in serum. The estimated Mr of the peak was 120 000, presumably representing one [125I]hGH bound to two binding sites. The binding specificities of the serum GHBP, the water-soluble GH-binding site and the GH receptor on IM-9 lymphocytes were identical. The binding affinities for 22 000 hGH and for 20 000 hGH of the serum GHBP were similar to the binding affinity of the water-soluble GH-binding site but lower than those of the cellular GH receptor. These findings show that the characteristics of the serum GHBP are comparable to those of the water-soluble GH-binding site released from IM-9 cells and support the hypothesis that in man the serum GHBP is produced by proteolytic cleavage of the cellular GH receptor.

scholarly journals An Essential Role of the CAAT/Enhancer Binding Protein-α in the Vitamin D-Induced Expression of the Human Steroid/Bile Acid-Sulfotransferase (SULT2A1)

2006 ◽  
Vol 20 (4) ◽  
pp. 795-808 ◽  
Author(s):  
Chung S. Song ◽  
Ibtissam Echchgadda ◽  
Young-Kyo Seo ◽  
Taesung Oh ◽  
Soyoung Kim ◽  
...  
Keyword(s):  
Vitamin D ◽  
Binding Site ◽  
Essential Role ◽  
Binding Protein ◽  
Water Soluble ◽  
Induced Expression ◽  
Composite Element ◽  
Deoxyribonuclease I ◽  
Enhancer Binding Protein

Abstract The vitamin D receptor (VDR) regulates steroid and drug metabolism by inducing the genes encoding phase I and phase II enzymes. SULT2A1 is a liver- and intestine-expressed sulfo-conjugating enzyme that converts the alcohol-OH of neutral steroids, bile acids, and drugs to water-soluble sulfated metabolites. 1α,25-Dihydroxyvitamin D3 [1,25-(OH)2D3] induces SULT2A1 gene transcription after the recruitment of VDR to the vitamin D-responsive chromatin region of SULT2A1. A composite element in human SULT2A1 directs the 1,25-(OH)2D3-mediated induction of natural and heterologous promoters. This element combines a VDR/retinoid X receptor-α-binding site [vitamin D response element (VDRE)], which is an imperfect inverted repeat 2 of AGCTCA, and a CAAT/enhancer binding protein (C/EBP)-binding site located 9 bp downstream to VDRE. The binding sites were identified by EMSA, antibody supershift, and deoxyribonuclease I footprinting. C/EBP-α at the composite element plays an essential role in the VDR regulation of SULT2A1, because 1) induction was lost for promoters with inactivating mutations at the VDRE or C/EBP element; 2) SULT2A1 induction by 1,25-(OH)2D3 in C/EBP-α-deficient cells required the expression of cotransfected C/EBP-α; and 3) C/EBP-β did not substitute for C/EBP-α in this regulation. VDR and C/EBP-α were recruited concurrently to the composite element along with the coactivators p300, steroid receptor coactivator 1 (SRC-1), and SRC-2, but not SRC-3. VDR and C/EBP-α associated endogenously as a DNA-dependent, coimmunoprecipitable complex, which was detected at a markedly higher level in 1,25-(OH)2D3-treated cells. These results provide the first example of the essential role of the interaction in cis between C/EBP-α and VDR in directing 1,25-(OH)2D3-induced expression of a VDR target gene.

Chlorophyll a/b binding-specificity in water-soluble chlorophyll protein

Nature Plants ◽  
2018 ◽  
Vol 4 (11) ◽  
pp. 920-929 ◽  
Author(s):  
Daniel M. Palm ◽  
Alessandro Agostini ◽  
Vivien Averesch ◽  
Philipp Girr ◽  
Mara Werwie ◽  
...  
Keyword(s):  
Chlorophyll A ◽  
Binding Specificity ◽  
Water Soluble ◽  
Chlorophyll Protein

Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis in NIH 3T3 cells

2000 ◽  
Vol 113 (21) ◽  
pp. 3805-3814 ◽  
Author(s):  
J. Xu ◽  
D. Ziemnicka ◽  
G.S. Merz ◽  
L. Kotula
Keyword(s):  
Fluorescent Dyes ◽  
Fluorescent Protein ◽  
Cultured Cells ◽  
Binding Protein ◽  
Sh3 Domain ◽  
Water Soluble ◽  
Protein Markers ◽  
3T3 Cells ◽  
Nih 3T3 ◽  
Nih 3T3 Cells

Macropinocytosis is an endocytic process that occurs through non-clathrin coated vesicles larger than 0.2 microm in diameter. Although macropinocytic vesicles are readily visualized in cultured cells by the introduction of fluorescent, water-soluble dyes into the culture medium, protein markers associated with this type of vesicles have not yet been well defined. Here, we report that human spectrin SH3 domain binding protein 1, or Hssh3bp1, associates with macropinosomes in NIH 3T3 fibroblasts. Hssh3bp1 macropinosomes are heterogeneous in morphology and size, do not endocytose transferrin and are resistant to brefeldin A treatment. Cytochalasin D, and wortmannin block endocytosis of fluorescent dyes into the Hssh3bp1 macropinosomes and dramatically affect their morphology. Overexpression of Hssh3bp1-green fluorescent protein abolished fusion of vesicles resulting in a decreased endocytosis of fluorescence dyes, thus suggesting a potential regulatory role of Hssh3bp1 in macropinocytosis. In the macropinosomes of NIH 3T3 cells, Hssh3bp1 associates with a 200-kDa protein that crossreacts with a monoclonal antibody to the erythroid alpha-spectrin SH3 domain. Thus macropinosomes in cells may contain a spectrin-like protein.

scholarly journals Electron Nuclear Double Resonance of the Chlorophyll Triplet State in the Water-Soluble Chlorophyll Protein from Brassica oleracea: Investigation of the Effect of the Binding Site on the Hyperfine Couplings

2020 ◽  
Vol 51 (9-10) ◽  
pp. 925-937
Author(s):  
Alessandro Agostini ◽  
Daniel M. Palm ◽  
Harald Paulsen ◽  
Marilena Di Valentin ◽  
Donatella Carbonera
Keyword(s):  
Triplet State ◽  
Brassica Oleracea ◽  
Double Resonance ◽  
Water Soluble ◽  
Triplet States ◽  
Triplet Energy ◽  
Electron Nuclear Double Resonance ◽  
Light Harvesting Complexes ◽  
Chlorophyll Protein ◽  
Hyperfine Couplings

Abstract An investigation of the photoexcited triplet state of chlorophyll (Chl) a in the water-soluble chlorophyll protein (WSCP) of Brassica oleracea has been carried out by means of electron-nuclear double resonance (ENDOR), achieving a complete assignment of the observed hyperfine couplings corresponding to methine protons and methyl groups of Chl a triplet state. The triplet-state properties, and in particular the hyperfine couplings, were found to be similar to those previously reported for Chl a in the WSCP of Lepidium virginicum. Therefore, the porphyrin ring deformation observed in Brassica oleracea WSCP seems to only slightly affect the spin density of 3Chl a. This may be relevant when considering the robustness of triplet–triplet energy transfer mechanisms, relying on wavefunction overlap, in systems, such as the photosynthetic light-harvesting complexes, in which Chl triplet states with distorted geometries are involved.

Molecular cloning and functional expression of a water-soluble chlorophyll-binding protein from Japanese wild radish

2013 ◽  
Vol 170 (4) ◽  
pp. 406-412 ◽  
Author(s):  
Shigekazu Takahashi ◽  
Mayuko Ono ◽  
Akira Uchida ◽  
Katsumi Nakayama ◽  
Hiroyuki Satoh
Keyword(s):  
Molecular Cloning ◽  
Binding Protein ◽  
Functional Expression ◽  
Water Soluble ◽  
Wild Radish

Isolation of water-soluble chlorophyll protein from the leaves of Chenopodium album

1963 ◽  
Vol 75 ◽  
pp. 293-298 ◽  
Author(s):  
Eijiro Yakushiji ◽  
Keigo Uchino ◽  
Yasutomo Sugimura ◽  
Irie Shiratori ◽  
Fusako Takamiya
Keyword(s):  
Chenopodium Album ◽  
Water Soluble ◽  
Chlorophyll Protein

scholarly journals The Crystal Structure of a Cyanobacterial Water-Soluble Carotenoid Binding Protein

Structure ◽  
2003 ◽  
Vol 11 (1) ◽  
pp. 55-65 ◽  
Author(s):  
Cheryl A Kerfeld ◽  
Michael R Sawaya ◽  
Vishnu Brahmandam ◽  
Duilio Cascio ◽  
Kwok Ki Ho ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Binding Protein ◽  
Water Soluble
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