来自SHORT-LEAF保存串联直接重复的类蛋白调节P.patens的细胞体发育

Seed structures are composed of a protective seed coat surrounding a plant embryo, and a food store for the developing embryo. The embryo contains the precursor tissues for leaves, stem, and roots. The endosperm and cotyledons—seed leaves—act as the food reserves for the growing embryo.

Asexual reproduction allows plants to reproduce without growing flowers, attracting pollinators, or dispersing seeds. Offspring are genetically identical to the parent and produced without the fusion of male and female gametes.

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...

Seedless Vascular Plants Were the First Tall Plants on Earth

Sporulation is a complex developmental process that allows certain Gram-positive bacteria, such as Bacillus subtilis and Clostridium species, to survive extreme environmental conditions. This process is tightly regulated by a series of signaling cascades and transcriptional controls, ensuring the formation of a highly resistant endospore.Sporulation is triggered by unfavorable conditions, such as nutrient depletion, and is governed by a phosphorelay system. One of the sensor kinases, such as...

Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.