Phosphorylation regulates mycobacterial proteasome

[1]  P. Datta,et al.  The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. , 2015, Microbiology.

[2]  F. Striebel,et al.  Pupylation as a signal for proteasomal degradation in bacteria. , 2014, Biochimica et biophysica acta.

[3]  Timothy J Jarome,et al.  CaMKII, but not protein kinase A, regulates Rpt6 phosphorylation and proteasome activity during the formation of long-term memories , 2013, Front. Behav. Neurosci..

[4]  D. Saucier,et al.  Enriched childhood experiences moderate age-related motor and cognitive decline , 2012, Front. Behav. Neurosci..

[5]  K. Chakraborty,et al.  Interaction of Mycobacterium tuberculosis Elongation Factor Tu with GTP Is Regulated by Phosphorylation , 2011, Journal of bacteriology.

[6]  Meetu Gupta,et al.  Phosphorylation of Mycobacterium tuberculosis Ser/Thr Phosphatase by PknA and PknB , 2011, PloS one.

[7]  J. Suh,et al.  Regulation of Polar Peptidoglycan Biosynthesis by Wag31 Phosphorylation in Mycobacteria , 2010, BMC Microbiology.

[8]  Jong-Bok Yoon,et al.  Osmotic Stress Inhibits Proteasome by p38 MAPK-dependent Phosphorylation* , 2010, The Journal of Biological Chemistry.

[9]  Sathya Narayanan Nagarajan,et al.  Phosphorylation of Enoyl-Acyl Carrier Protein Reductase InhA Impacts Mycobacterial Growth and Survival* , 2010, The Journal of Biological Chemistry.

[10]  W. Bishai,et al.  "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. , 2010, Molecular cell.

[11]  Vandana Malhotra,et al.  Mycobacterium tuberculosis protein kinase K confers survival advantage during early infection in mice and regulates growth in culture and during persistent infection: implications for immune modulation , 2010, Microbiology.

[12]  Tao Wang,et al.  Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation , 2010, Nature Structural &Molecular Biology.

[13]  S. Gygi,et al.  Correction: Prokaryotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis , 2010, PLoS ONE.

[14]  J. Maupin-Furlow,et al.  Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon Haloferax volcanii , 2010, Archaea.

[15]  Tao Wang,et al.  Structural basis for the assembly and gate closure mechanisms of the Mycobacterium tuberculosis 20S proteasome , 2010, The EMBO journal.

[16]  F. Striebel,et al.  The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N‐terminus , 2010, The EMBO journal.

[17]  Vineet Bafna,et al.  Expansion of the mycobacterial "PUPylome". , 2010, Molecular bioSystems.

[18]  Julian Mintseris,et al.  Prokayrotic Ubiquitin-Like Protein (Pup) Proteome of Mycobacterium tuberculosis , 2010, PloS one.

[19]  B. Kan,et al.  Virulence regulator AphB enhances toxR transcription in Vibrio cholerae , 2010, BMC Microbiology.

[20]  M. Sutter,et al.  Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes , 2009, Nature Structural &Molecular Biology.

[21]  P. Dorrestein,et al.  Proteasomal Protein Degradation in Mycobacteria Is Dependent upon a Prokaryotic Ubiquitin-like Protein* , 2009, Journal of Biological Chemistry.

[22]  S. Gygi,et al.  Ubiquitin-Like Protein Involved in the Proteasome Pathway of Mycobacterium tuberculosis , 2008, Science.

[23]  M. Thakur,et al.  Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis. , 2008, The Biochemical journal.

[24]  J. Suh,et al.  Wag31, a homologue of the cell division protein DivIVA, regulates growth, morphology and polar cell wall synthesis in mycobacteria. , 2008, Microbiology.

[25]  W. Hillen,et al.  In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice , 2007, Nature Medicine.

[26]  Ping Huang,et al.  Proteasome Function Is Regulated by Cyclic AMP-dependent Protein Kinase through Phosphorylation of Rpt6* , 2007, Journal of Biological Chemistry.

[27]  G. Schoofs,et al.  Proteome analysis of Streptomyces coelicolor mutants affected in the proteasome system reveals changes in stress-responsive proteins , 2007, Archives of Microbiology.

[28]  Soo Chan Lee,et al.  A novel interaction between N‐myristoylation and the 26S proteasome during cell morphogenesis , 2007, Molecular microbiology.

[29]  M. Thakur,et al.  GTPase Activity of Mycobacterial FtsZ Is Impaired Due to Its Transphosphorylation by the Eukaryotic-type Ser/Thr Kinase, PknA* , 2006, Journal of Biological Chemistry.

[30]  S. Butler-Wu,et al.  Identification of substrates of the Mycobacterium tuberculosis proteasome , 2006, The EMBO journal.

[31]  W. Bishai,et al.  Deletion of a Mycobacterium tuberculosis proteasomal ATPase homologue gene produces a slow-growing strain that persists in host tissues. , 2006, The Journal of infectious diseases.

[32]  M. Hochstrasser,et al.  Modification of proteins by ubiquitin and ubiquitin-like proteins. , 2006, Annual review of cell and developmental biology.

[33]  Amit Singh,et al.  Dissecting virulence pathways of Mycobacterium tuberculosis through protein-protein association. , 2006, Proceedings of the National Academy of Sciences of the United States of America.

[34]  T. Parsons,et al.  Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity , 2006, Molecular microbiology.

[35]  Huilin Li,et al.  Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate , 2006, Molecular microbiology.

[36]  S. Cole,et al.  Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA domain-containing protein, through activation loop-mediated interactions. , 2005, Journal of molecular biology.

[37]  L. Cantley,et al.  The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. , 2005, Genes & development.

[38]  R. Horiguchi,et al.  Identification of a protein kinase which phosphorylates a subunit of the 26S proteasome and changes in its activity during meiotic cell cycle in goldfish oocytes. , 2005, Cellular signalling.

[39]  S. French,et al.  Hyperphosphorylation of rat liver proteasome subunits: the effects of ethanol and okadaic acid are compared. , 2004, Life sciences.

[40]  G. Hart,et al.  O-GlcNAc modification: a nutritional sensor that modulates proteasome function. , 2004, Trends in cell biology.

[41]  A. Rivett,et al.  Phosphorylation of 20S proteasome alpha subunit C8 (alpha7) stabilizes the 26S proteasome and plays a role in the regulation of proteasome complexes by gamma-interferon. , 2004, The Biochemical journal.

[42]  W. Baumeister,et al.  Crystal structures of the Rhodococcus proteasome with and without its pro-peptides: implications for the role of the pro-peptide in proteasome assembly. , 2004, Journal of molecular biology.

[43]  A. Rivett,et al.  Phosphorylation of proteasomes in mammalian cells , 1999, Molecular Biology Reports.

[44]  R. Puvanakrishnan,et al.  Fate of Mycobacterium tuberculosis inside rate peritoneal macrophages in vitro , 1997, Molecular and Cellular Biochemistry.

[45]  A. Rivett,et al.  Phosphorylation of 20 S proteasome alpha subunit C 8 ( α 7 ) stabilizes the 26 S proteasome and plays a role in the regulation of proteasome complexes by γ-interferon , 2004 .

[46]  C. Nathan,et al.  The Proteasome of Mycobacterium tuberculosis Is Required for Resistance to Nitric Oxide , 2003, Science.

[47]  R. Husson,et al.  RshA, an anti‐sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH , 2003, Molecular microbiology.

[48]  L. Netto,et al.  20 S Proteasome from Saccharomyces cerevisiae Is Responsive to Redox Modifications and IsS-Glutathionylated* , 2003, The Journal of Biological Chemistry.

[49]  P. Zwickl.  The 20S proteasome. , 2002, Current topics in microbiology and immunology.

[50]  M. Spillantini,et al.  α‐Synuclein metabolism and aggregation is linked to ubiquitin‐independent degradation by the proteasome , 2001, FEBS letters.

[51]  A. Rivett,et al.  Regulation of proteasome complexes by γ-interferon and phosphorylation , 2001 .

[52]  H. Yokosawa,et al.  Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. , 2001, Biochemistry.

[53]  Yayoi Kimura,et al.  N α-Acetylation and Proteolytic Activity of the Yeast 20 S Proteasome* , 2000, The Journal of Biological Chemistry.

[54]  W Baumeister,et al.  Proteasomes and other self-compartmentalizing proteases in prokaryotes. , 1999, Trends in microbiology.

[55]  Simon Paul,et al.  Mycobacterium tuberculosis Catalase and Peroxidase Activities and Resistance to Oxidative Killing in Human Monocytes In Vitro , 1999, Infection and Immunity.

[56]  W. Baumeister,et al.  The 26S proteasome: a molecular machine designed for controlled proteolysis. , 1999, Annual review of biochemistry.

[57]  E. Koonin,et al.  Novel families of putative protein kinases in bacteria and archaea: evolution of the "eukaryotic" protein kinase superfamily. , 1998, Genome research.

[58]  W. Baumeister,et al.  Dissecting the assembly pathway of the 20S proteasome , 1997, FEBS letters.

[59]  T. E. Shrader,et al.  Inactivation of the 20S proteasome in Mycobacterium smegmatis , 1997, Molecular microbiology.

[60]  R. Huber,et al.  Structure of 20S proteasome from yeast at 2.4Å resolution , 1997, Nature.

[61]  J. D. Etlinger,et al.  Phosphorylation of the proteasome activator PA28 is required for proteasome activation. , 1996, Biochemical and biophysical research communications.

[62]  A. Rivett,et al.  Phosphorylation of proteasomes in mammalian cells. Identification of two phosphorylated subunits and the effect of phosphorylation on activity. , 1996, European journal of biochemistry.

[63]  R. Kornberg,et al.  Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK , 1994, Cell.