The synthesis of the novel ligand tris(2,2¢-bipyrid-6-yl) methanol (L 1 ) is described. Co-ordination of the ligand to the first row transition metals (Mn 2+ -Zn 2+ ) as well as Cd 2+ showed that the ligand formed complexes close to trigonal prismatic in geometry in the solid state. Analysis of the geometry of the co-ordination spheres showed varying degrees of trigonal prismatic and octahedral character. For each d-electron configuration, this could be related to the relative differences in ligand field stabilisation energies for the two geometries.

The term "ultrawideband" (UWB) in antenna research has become a buzzword over the past decade.

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RNA Polymerase II (RNAPII) uniquely possesses an extended carboxy terminal domain (CTD) on its largest subunit, Rpb1, comprising a repetitive Tyr1Ser2Pro3Thr4 Ser5Pro6Ser7 motif with potential phosphorylation sites. The phosphorylation of the CTD serves as a signal for the binding of various transcription regulators for mRNA biogenesis including the mRNA capping complex. In eukaryotes, the 5 prime capping of the nascent transcript is the first detectable mRNA processing event, and is crucial for the productive transcript elongation. The binding of capping enzyme, RNA guanylyltransferases to the transcribing RNAPII is known to be primarily facilitated by the CTD, phosphorylated at Ser5 (Ser5P). Here we report that the Saccharomyces cerevesiae RNA guanylyltransferase (Ceg1) has dual specificity and interacts not only with Ser5P but also with Ser7P of the CTD. The Ser7 of CTD is essential for the unconditional growth and efficient priming of the mRNA capping complex. The Arg159 and Arg185 of Ceg1 are the key residues that interact with the Ser5P, while the Lys175 with Ser7P of CTD. These interactions appear to be in a specific pattern of Ser5PSer7PSer5P in a tri-heptad CTD (YSPTSPPS YSPTSPSP YSPTSPPS) and provide molecular insights into the Ceg1-CTD interaction for mRNA transcription.

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