Laboratory of Molecular Biology

About: Laboratory of Molecular Biology is a facility organization based out in Cambridge, Cambridgeshire, United Kingdom. It is known for research contribution in the topics: Gene & RNA. The organization has 19395 authors who have published 24236 publications receiving 2101480 citations.

Molecular cloning of sequences from wingless, a segment polarity gene in Drosophila: the spatial distribution of a transcript in embryos.

Abstract: In Drosophila the process of segmentation depends on the function of coordinate, gap, pair-rule and segment-polarity genes. Mutations in segment-polarity genes cause defects in the pattern of every segment. Here the cloning of sequences from a segment-polarity gene, wingless, and the in situ localization of a transcript in embryos are described. The transcript is first detected in the anterior and posterior regions of the blastoderm embryo at cellularization, and accumulates in a series of stripes in the extended germ band, one stripe per metameric unit. Each stripe is localized to the most posterior cells of each parasegment. The signal is predominantly epidermal, and transcript accumulates only transiently in the mesoderm and nervous system. This pattern of expression is discussed with respect to models of pattern formation in segmental units.

Developmental and evolutionary diversity of plant MADS-domain factors: insights from recent studies

Abstract: Members of the MADS-box transcription factor family play essential roles in almost every developmental process in plants. Many MADS-box genes have conserved functions across the flowering plants, but some have acquired novel functions in specific species during evolution. The analyses of MADS-domain protein interactions and target genes have provided new insights into their molecular functions. Here, we review recent findings on MADS-box gene functions in Arabidopsis and discuss the evolutionary history and functional diversification of this gene family in plants. We also discuss possible mechanisms of action of MADS-domain proteins based on their interactions with chromatin-associated factors and other transcriptional regulators.

Solution structure of the DNA-binding domain of the oestrogen receptor.

Abstract: STEROID hormone receptors control gene expression through binding, as dimers, to short palindromic response elements located upstream of the genes they regulate1–3. An independent domain of ∼70 amino acids directs this sequence-specific DNA binding and is highly conserved between different receptor proteins and related transcription factors4–6. This domain contains two zinc-binding Cys2–Cys2 sequence motifs, which loosely resemble the 'zinc-finger' motifs of TFIIIA7–10. Here we describe the structure of the DNA-binding domain from the oestrogen receptor, as determined by two-dimensional 1H NMR techniques. The two 'zinc-finger'-like motifs fold to form a single structural domain and are thus distinct from the independently folded units of the TFIIIA-type zinc fingers11–13. The structure consists of two helices perpendicular to each other. A zinc ion, coordinated by four conserved cysteines, holds the base of a loop at the N terminus of each helix. This novel structural domain seems to be a general structure for protein-DNA recognition.