Inter- and under-canopy soil water, leaf-level and whole-plant gas exchange dynamics of a semi-arid perennial C4 grass.

It is not clear if tree canopies in savanna ecosystems exert positive or negative effects on soil moisture, and how these might affect understory plant carbon balance. To address this, we quantified rooting-zone volumetric soil moisture (θ(25 cm)), plant size, leaf-level and whole-plant gas exchange of the bunchgrass, bush muhly (Muhlenbergia porteri), growing under and between mesquite (Prosopis velutina) in a southwestern US savanna. Across two contrasting monsoon seasons, bare soil θ(25 cm) was 1.

Arginine methylation of scaffold attachment factor A by heterogeneous nuclear ribonucleoprotein particle-associated PRMT1.

Components of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex and other nucleic acid-binding proteins are subject to methylation on specific arginine residues by the catalytic activity of arginine methyltransferases. The methylation has been implicated in transcriptional regulation and RNA and protein trafficking and signal transduction, but the mechanism by which these functions are achieved has remained undetermined. We show here that the predominant arginine methyltransferase in human cells, protein arginine methyltransferase 1 (PRMT1), is associated with hnRNP complexes, dependent on the methylation status of the cell, and that it methylates its preferred substrates in situ.

Protein kinase CK2 differentially phosphorylates maize chromosomal high mobility group B (HMGB) proteins modulating their stability and DNA interactions.

The high mobility group (HMG) proteins of the HMGB family are architectural factors in eukaryotic chromatin, which are involved in the regulation of various DNA-dependent processes. We have examined the post-translational modifications of five HMGB proteins from maize suspension cultured cells, revealing that HMGB1 and HMGB2/3, but not HMGB4 and HMGB5, are phosphorylated by protein kinase CK2. The phosphorylation sites have been mapped to the acidic C-terminal domains by analysis of tryptic peptides derived from HMGB1 and HMGB2/3 using nanospray ion trap mass spectrometry.