TITLE

Probing the N-terminal sequence of spinach PsbO: evidence that essential threonine residues bind to different functional sites in eukaryotic photosystem II

AUTHOR(S)
Popelka, Hana; Yocum, Charles
PUB. DATE
June 2012
SOURCE
Photosynthesis Research;Jun2012, Vol. 112 Issue 2, p117
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
The N-terminal E−L domain of the manganese-stabilizing protein (PsbO) from spinach prevents non-specific binding of the subunit to photosystem II (PSII) and deletions of the E−T or E−T sequences from the PsbO N-terminus reduce or impair, respectively, functional binding of PsbO to PSII (Popelkova et al., Biochemistry 42:6193-6200, ). The work presented here provides deeper insights into the interaction of PsbO with PSII. The data show that a single mutation, T → A in mature PsbO from spinach reduces the stoichiometry of its functional binding from two to one subunit per PSII and decreases reconstitution of activity to about 45 % of the wild-type control. Replacement of the E−L domain with M in the T15A PsbO mutant has no additional negative effect on recovery of O evolution activity, but it significantly weakens both functional and nonspecific binding of the truncated mutant to PSII. These results suggest that the T side-chain by itself is essential for binding of one of two PsbO subunits to eukaryotic PSII and that specific PSII-binding sites for PsbO are distinguishable; one PSII-binding site does not require PsbO-T and probably interacts with the other N-terminal domain of PsbO. Identity of the latter domain is revealed by a requirement for the presence of the E−L sequence that is shown here to be necessary for high-affinity binding of PsbO to PSII. When combined with previous results, the data presented here lead to a more detailed model for PsbO binding in eukaryotic PSII.
ACCESSION #
76351049

 

Related Articles

  • CD spectroscopy of peptides and proteins bound to large unilamellar vesicles. Ladokhin, Alexey S.; Fernández-Vidal, Mónica; White, Stephen H.; Fernández-Vidal, Mónica // Journal of Membrane Biology;Aug2010, Vol. 236 Issue 3, p247 

    Circular dichroism (CD) spectroscopy is an essential tool for determining the conformation of proteins and peptides in membranes. It can be particularly useful for measuring the free energy of partitioning of peptides into lipid vesicles. The belief is broadly held that such CD measurements can...

  • The Role of Ile476 in the Structural Stability and Substrate Binding of Human Cytochrome P450 2C8. Lu Sun; Zhong-Hua Wang; Feng-Yun Ni; Xiang-Shi Tan; Zhong-Xian Huang // Protein Journal;Jan2010, Vol. 29 Issue 1, p32 

    Abstract  The biological function and stability of a cytochrome P450 (CYP) mainly depend on the subtle properties of the residues in the active site cavity, which are generally more divergent among proteins than other parts of the protein. As the most unique member of human CYP2C...

  • Identification of archaeal proteins that affect the exosome function in vitro. Luz, Juliana S.; Ramos, Celso R. R .; Santos, Márcia C. T.; Coltri, Patricia P.; Palhano, Fernando L.; Foguel, Debora; Zanchin, Nilson I. T.; Oliveira, Carla C. // BMC Biochemistry;2010, Vol. 11, p22 

    Background: The archaeal exosome is formed by a hexameric RNase PH ring and three RNA binding subunits and has been shown to bind and degrade RNA in vitro. Despite extensive studies on the eukaryotic exosome and on the proteins interacting with this complex, little information is yet available...

  • Crystal Structure of Eucaryotic E3, Lipoamide Dehydrogenase from Yeast1. Toyoda, Tomohiko; Suzuki, Kaoru; Sekiguchi, Takeshi; Reed, Lester J.; Takenaka, Akio // Journal of Biochemistry;1998, Vol. 123 Issue 4, p668 

    The crystal structure of eucaryotic lipoamide dehydrogenase from yeast has been determined by an X-ray analysis at 2.7 (partially at 2.4) A resolution. The enzyme has two identical subunits related by a pseudo twofold symmetry. The tertiary structure is similar to those of other procaryotic...

  • Expression and genomic analysis of midasin, a novel and highly conserved AAA protein distantly related to dynein. Garbarino, Joan E.; Gibbons, I. R. // BMC Genomics;2002, Vol. 3, p18 

    Background: The largest open reading frame in the Saccharomyces genome encodes midasin (MDN1p, YLR106p), an AAA ATPase of 560 kDa that is essential for cell viability. Orthologs of midasin have been identified in the genome projects for Drosophila, Arabidopsis, and Schizosaccharomyces pombe....

  • Membrane Crystals of Plant Light-Harvesting Complex II Disassemble Reversibly in Light. Hind, Geoffrey; Wall, Joseph S.; Várkonyi, Zsuzsanna; Istokovics, Anita; Lambrev, Petar H.; Garab, Győző // Plant & Cell Physiology;Jul2014, Vol. 55 Issue 7, p1296 

    Using the mass-measuring capability of scanning transmission electron microscopy, we demonstrate that membrane crystals of the main light-harvesting complex of plants possess the ability to undergo light-induced dark-reversible disassociations, independently of the photochemical apparatus. This...

  • Two Distantly Spaced Basic Patches in the Flexible Domain of Huntingtin-Interacting Protein 1 (HIP1) Are Essential for the Binding of Clathrin Light Chain. Ybe, Joel A.; Clegg, Mary E.; Illingworth, Melissa; Gonzalez, Claire; Qian Niu // Biochemistry Research International;2009, p1 

    The interaction between HIP family proteins (HIP1 and HIP12/1R) and clathrin is fundamental to endocytosis. We used circular dichroism (CD) to study the stability of an HIP1 subfragment (aa468-530) that is splayed open. CD thermal melts show HIP1 468-530 is only stable at low temperatures, but...

  • Yeast hexokinase isoenzyme ScHxk2: stability of a two-domain protein with discontinuous domains. Lilie, Hauke; Bär, Dorit; Kettner, Karina; Weininger, Ulrich; Balbach, Jochen; Naumann, Manfred; Müller, Eva-Christina; Otto, Albrecht; Gast, Klaus; Golbik, Ralph; Kriegel, Thomas // PEDS: Protein Engineering, Design & Selection;Jan2011, Vol. 24 Issue 1/2, p79 

    The hexokinase isoenzyme 2 of Saccharomyces cerevisiae (ScHxk2) represents an archetype of a two-domain protein with the active site located in a cleft between the two domains. Binding of the substrate glucose results in a rigid body movement of the two domains leading to a cleft closure of the...

  • Good cap/bad cap: how the cap-binding complex determines RNA fate. Müller-McNicoll, Michaela; Neugebauer, Karla M // Nature Structural & Molecular Biology;Jan2014, Vol. 21 Issue 1, p9 

    The article discusses studies on the association of cap-binding complex (CBC) with RNA polymerase II transcripts. The existence of arsenite resistance protein 2 (ARS2) in CBC complexes is mentioned. The use of affinity capture MS (ACMS) method in evaluating CBC interactions and their...

Share

Read the Article

Courtesy of MICHIGAN ELIBRARY

Sorry, but this item is not currently available from your library.

Try another library?
Sign out of this library

Other Topics