47 research outputs found
Membrane organization of photosystem I complexes in the most abundant phototroph on Earth
Prochlorococcus is a major contributor to primary production, and globally the most abundant photosynthetic genus of picocyanobacteria because it can adapt to highly stratified low-nutrient conditions that are characteristic of the surface ocean. Here, we examine the structural adaptations of the photosynthetic thylakoid membrane that enable different Prochlorococcus ecotypes to occupy high-light, low-light and nutrient-poor ecological niches. We used atomic force microscopy to image the different photosystem I (PSI) membrane architectures of the MED4 (high-light) Prochlorococcus ecotype grown under high-light and low-light conditions in addition to the MIT9313 (low-light) and SS120 (low-light) Prochlorococcus ecotypes grown under low-light conditions. Mass spectrometry quantified the relative abundance of PSI, photosystem II (PSII) and cytochrome b6f complexes and the various Pcb proteins in the thylakoid membrane. Atomic force microscopy topographs and structural modelling revealed a series of specialized PSI configurations, each adapted to the environmental niche occupied by a particular ecotype. MED4 PSI domains were loosely packed in the thylakoid membrane, whereas PSI in the low-light MIT9313 is organized into a tightly packed pseudo-hexagonal lattice that maximizes harvesting and trapping of light. There are approximately equal levels of PSI and PSII in MED4 and MIT9313, but nearly twofold more PSII than PSI in SS120, which also has a lower content of cytochrome b6f complexes. SS120 has a different tactic to cope with low-light levels, and SS120 thylakoids contained hundreds of closely packed Pcb–PSI supercomplexes that economize on the extra iron and nitrogen required to assemble PSI-only domains. Thus, the abundance and widespread distribution of Prochlorococcus reflect the strategies that various ecotypes employ for adapting to limitations in light and nutrient levels
A Review of Controlling Motivational Strategies from a Self-Determination Theory Perspective: Implications for Sports Coaches
The aim of this paper is to present a preliminary taxonomy of six controlling strategies, primarily based on the parental and educational literatures, which we believe are employed by coaches in sport contexts. Research in the sport and physical education literature has primarily focused on coaches’ autonomysupportive behaviours. Surprisingly, there has been very little research on the use of controlling strategies. A brief overview of the research which delineates each proposed strategy is presented, as are examples of the potential manifestation of the behaviours associated with each strategy in the context of sports coaching. In line with self-determination theory (Deci & Ryan, 1985; Ryan & Deci, 2002), we propose that coach behaviours employed to pressure or control athletes have the potential to thwart athletes’ feelings of autonomy, competence,and relatedness, which, in turn, undermine athletes’ self-determined motivation and contribute to the development of controlled motives. When athletes feel pressured to behave in a certain way, a variety of negative consequences are expected to ensue which are to the detriment of the athletes’ well-being. The purpose of this paper is to raise awareness and interest in the darker side of sport participation and to offer suggestions for future research in this area
The Relationship Between Implicit Beliefs, Anxiety, and Attributional Style in High-Level Soccer Players
Development of a Transient Mammalian Expression Process for the Production of the Cancer Testis Antigen NY-ESO-1
Cloning and characterization of TNKL, a member of tankyrase gene family.
By serological screening of a breast tumor cDNA library we have identified a novel human gene, tnkl, encoding an ankyrin-related protein with a high degree of similarity to tankyrase, the poly(ADP-ribose)polymerase associated with human telomeres (Smith et al, Science 282: 1484). The tnkl gene maps to chromosome 10, while the tnks gene encoding tankyrase is located on chromosome 8. The predicted 1166-aa protein product of the tnkl gene is 78% identical to human tankyrase and 62% to a putative D. melanogaster protein. Since the proteins have essentially identical domain structures, the corresponding genes form a distinct gene family. The possible link between TNKL and cancer justifies its further functional analysis