Protein kinase Akt2/PKBβ is involved in blastomere proliferation of preimplantation mouse embryos

Activation of Akt/Protein Kinase B (PKB) by phosphatidylinositol-3-kinase (PI3K) controls several cellular functions largely studied in mammalian cells, including preimplantation embryos. We previously showed that early mouse embryos inherit active Akt from oocytes and that the intracellular localization of this enzyme at the two-cell stage depends on the T-cell leukemia/lymphoma 1 oncogenic protein, Tcl1. We have now investigated whether Akt isoforms, namely Akt1, Akt2 and Akt3, exert a specific role in blastomere proliferation during preimplantation embryo development. We show that, in contrast to other Akt family members, Akt2 enters male and female pronuclei of mouse preimplantation embryos at the late one-cell stage and thereafter maintains a nuclear localization during later embryo cleavage stages. Depleting one-cell embryos of single Akt family members by microinjecting Akt isoform-specific antibodies into wild-type zygotes, we observed that: (a) Akt2 is necessary for normal embryo progression through cleavage stages; and (b) the specific nuclear targeting of Akt2 in two-cell embryos depends on Tcl1. Our results indicate that preimplantation mouse embryos have a peculiar regulation of blastomere proliferation based on the activity of the Akt/PKB family member Akt2, which is mediated by the oncogenic protein Tcl1. Both Akt2 and Tcl1 are essential for early blastomere proliferation and embryo development.     

Environmental assessment of maize production alternatives: Traditional,intensive and GMO-based cropping patterns

The evolution of maize production patterns in Argentina is evaluated over the last 25 years to compare costs, benefits, environmental performance and sustainability as well as to identify the main driving sources and improvement potential. Results from Argentina cropping systems are compared to other systems worldwide in order to put the Argentina results in a broader context. The study focuses on three farming categories: (1) traditional, low-intensity systems, (2) conventional, high-intensity systems, and (3) GMO-based cropping systems. Low input intensity systems include traditional cropping patterns with seed selection by farmers and conventional hybrid seed coupled to plowing and crop-animal rotation techniques; high input intensity systems use conventional hybrid seeds and recommended chemicals, irrigation and machinery with important soil erosion consequences; and GMO-based cropping systems use herbicide resistant transgenic hybrids, pesticides, higher fertilizer rates, and no-till practices. In each of the three cases, input flows are compared to the achieved yield (in mass and income terms) to better understand relative efficiencies and options for improvement. The study of GMO systems required a preliminary investigation of GMO seed production by seed companies, where a large investment in terms of prior knowledge and high-tech laboratory research is required. The assessments used the Emergy Accounting (EMA) approach. EMA includes material, energy, labor, money, and knowledge flows into the assessment and expands its focus over larger time and spatial scales than conventional economic and cumulative energy demand methods. Emergy-based environmental indicators of grain production for high-intensity hybrid and GMO systems both show a lower performance than low-intensity, traditional patterns in terms of resource return, renewability and sustainability. The fraction of renewability in low-intensity systems is between 28% and 63%, while it is between 8% and 26% for high-intensity hybrid and GMO systems. Calculated indicators also show that GMO-based maize production patterns do not guarantee the expected improvement over conventional high-intensity cropping systems or low-intensity systems in terms of performance and sustainability. Strong reliance on nonrenewable resources and technology, as well as role of direct and indirect labor costs are important factors in determining long-term sustainability and environmental stability of maize production systems.     

The structure and function of phytochrome A: the roles of the entire molecule and of its various parts

Phytochrome A is readily cleavable by proteolytic agents to yield an amino-terminal fragment of 66 kilodalton (kDa), which consists of residues 1 to approximately 600, and a dimer of the carboxy-terminal 55-kDa fragment, from residue 600 or so to the carboxyl terminus. The former domain, carrying the tetrapyrrole chromophore, has been studied extensively because of its photoactivity, while less attention has been paid to the non-chromophoric portion until quite recently. However, the evidence gathered to date suggests that this domain is also of great improtance. We present here a review of the structure and the biochemical and physiological functions of the two domains, of parts of these domains, and of the cooperation between them.     

Evolutionarily conserved midbody remodeling precedes ring canal formation during gametogenesis

1. Download : Download high-res image (194KB)
2. Download : Download full-size image

     

Mice Reach Higher Visual Sensitivity at Night by Using a More Efficient Behavioral Strategy

1. Download : Download high-res image (170KB)
2. Download : Download full-size image

     

The MDM2 RING Domain and Central Acidic Domain Play Distinct Roles in MDM2 Protein Homodimerization and MDM2-MDMX Protein Heterodimerization

The oncoprotein murine double minute 2 (MDM2) is an E3 ligase that plays a prominent role in p53 suppression by promoting its polyubiquitination and proteasomal degradation. In its active form, MDM2 forms homodimers as well as heterodimers with the homologous protein murine double minute 4 (MDMX), both of which are thought to occur through their respective C-terminal RING (really interesting new gene) domains. In this study, using multiple MDM2 mutants, we show evidence suggesting that MDM2 homo- and heterodimerization occur through distinct mechanisms because MDM2 RING domain mutations that inhibit MDM2 interaction with MDMX do not affect MDM2 interaction with WT MDM2. Intriguingly, deletion of a portion of the MDM2 central acidic domain selectively inhibits interaction with MDM2 while leaving intact the ability of MDM2 to interact with MDMX and to ubiquitinate p53. Further analysis of an MDM2 C-terminal deletion mutant reveals that the C-terminal residues of MDM2 are required for both MDM2 and MDMX interaction. Collectively, our results suggest a model in which MDM2-MDMX heterodimerization requires the extreme C terminus and proper RING domain structure of MDM2, whereas MDM2 homodimerization requires the extreme C terminus and the central acidic domain of MDM2, suggesting that MDM2 homo- and heterodimers utilize distinct MDM2 domains. Our study is the first to report mutations capable of separating MDM2 homo- and heterodimerization.     

Formation of a Tree having a Low Lignin Content

Received 30 September 2001/ Accepted in revised form 26 October 2001