Scholars@Duke
Arno Lee Greenleaf

Arno Lee Greenleaf

Professor Emeritus of Biochemistry
Biochemistry
arno@duke.edu
Duke Box 3711, Durham, NC 27710
0034 CARL Building, Duke Box 3711, Durham, NC 27710

Featured Works

The RNA polymerase II CTD kinase CTDK-I affects pre-mRNA 3' cleavage/polyadenylation through the processing component Pti1p.

Journal article Mol Cell · December 2002 Featured Publication There are several kinases in Saccharomyces cerevisiae that phosphorylate the CTD of RNA polymerase II, but specific and distinct functions of the phospho-CTDs generated by the different kinases are not well understood. A genetic screen for suppressors of l ... Full text Link to item Cite

Hyperphosphorylated C-terminal repeat domain-associating proteins in the nuclear proteome link transcription to DNA/chromatin modification and RNA processing.

Journal article Mol Cell Proteomics · August 2002 Featured Publication Using an interaction blot approach to search in the human nuclear proteome, we identified eight novel proteins that bind the hyperphosphorylated C-terminal repeat domain (phosphoCTD) of RNA polymerase II. Unexpectedly, five of the new phosphoCTD-associatin ... Full text Link to item Cite

Co-transcriptional splicing of pre-messenger RNAs: considerations for the mechanism of alternative splicing.

Journal article Gene · October 17, 2001 Featured Publication Nascent transcripts are the true substrates for many splicing events in mammalian cells. In this review we discuss transcription, splicing, and alternative splicing in the context of co-transcriptional processing of pre-mRNA. The realization that splicing ... Full text Link to item Cite

Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.

Journal article Biochemistry · July 24, 2001 Featured Publication The yeast prolyl isomerase, Ess1, has recently been shown to interact via its WW domain with the hyperphosphorylated form of the RNA polymerase II C-terminal domain (CTD). We have investigated folding of the Ess1 WW domain and its binding to peptides repre ... Full text Link to item Cite

The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II.

Journal article J Biol Chem · December 22, 2000 Featured Publication We showed previously that the WW domain of the prolyl isomerase, Ess1, can bind the phosphorylated carboxyl-terminal domain (phospho-CTD) of the largest subunit of RNA Polymerase II. Analysis of phospho-CTD binding by four other WW domain-containing Saccha ... Full text Link to item Cite

Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II.

Journal article Proc Natl Acad Sci U S A · August 1, 2000 Featured Publication An approach for purifying nuclear proteins that bind directly to the hyperphosphorylated C-terminal repeat domain (CTD) of RNA polymerase II was developed and used to identify one human phosphoCTD-associating protein as CA150. CA150 is a nuclear factor imp ... Full text Link to item Cite

Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation.

Journal article J Biol Chem · October 29, 1999 Featured Publication A phospho-carboxyl-terminal domain (CTD) affinity column created with yeast CTD kinase I and the CTD of RNA polymerase II was used to identify Ess1/Pin1 as a phospho-CTD-binding protein. Ess1/Pin1 is a peptidyl prolyl isomerase involved in both mitotic reg ... Full text Link to item Cite

Modulation of RNA polymerase II elongation efficiency by C-terminal heptapeptide repeat domain kinase I.

Journal article J Biol Chem · April 25, 1997 Featured Publication Hyperphosphorylation of the C-terminal heptapeptide repeat domain (CTD) of the RNA polymerase II largest subunit has been suggested to play a key role in regulating transcription initiation and elongation. To facilitate investigating functional consequence ... Full text Link to item Cite

The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent cyclin-cyclin-dependent kinase complex.

Journal article Mol Cell Biol · October 1995 Featured Publication Saccharomyces cerevisiae CTDK-I is a protein kinase complex that specifically and efficiently hyperphosphorylates the carboxyl-terminal repeat domain (CTD) of RNA polymerase II and is composed of three subunits of 58, 38, and 32 kDa. The kinase is essentia ... Full text Link to item Cite

Locus-specific variation in phosphorylation state of RNA polymerase II in vivo: correlations with gene activity and transcript processing.

Journal article Genes Dev · December 1993 Featured Publication To investigate functional differences between RNA polymerases IIA and IIO (Pol IIA and Pol IIO), with hypo- and hyperphosphorylated carboxy-terminal repeat domains (CTDs), respectively, we have visualized the in vivo distributions of the differentially pho ... Full text Link to item Cite

Positive patches and negative noodles: linking RNA processing to transcription?

Journal article Trends Biochem Sci · April 1993 Featured Publication A speculative model is presented that proposes specific mechanisms for effecting co-transcriptional splice site selection in pre-mRNAs. The model envisions that certain splicing factors containing arginine-rich, positively charged regions bind via these po ... Full text Link to item Cite

CTD kinase large subunit is encoded by CTK1, a gene required for normal growth of Saccharomyces cerevisiae.

Journal article Gene Expr · May 1991 Featured Publication We previously purified a yeast protein kinase that specifically hyperphosphorylates the carboxyl-terminal repeat domain (CTD) of RNA polymerase II largest subunit and showed that this CTD kinase consists of three subunits of 58, 38, and 32 kDa. We have now ... Link to item Cite