How Integration of Positive and Negative Regulatory Signals by a STAND Signaling Protein Depends on ATP Hydrolysis

Molecular Cell

Volumn 28, Issue 2, 2007, Pages 187-199

  Marquenet, Emélie ^a   Richet, Evelyne ^a  

^a INSTITUT PASTEUR   (France)

Author keywords

MICROBIO; SIGNLAING

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CASPASE RECRUITMENT DOMAIN PROTEIN 15; MALTOSE; PROTEIN; PROTEIN STAND; UNCLASSIFIED DRUG;

ARTICLE; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; HUMAN; HYDROLYSIS; NONHUMAN; NUCLEOTIDE METABOLISM; REGULON; SIGNAL TRANSDUCTION; STOICHIOMETRY;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ATP-BINDING CASSETTE TRANSPORTERS; CYSTATHIONINE GAMMA-LYASE; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FEEDBACK, BIOCHEMICAL; HYDROLYSIS; MULTIPROTEIN COMPLEXES; MUTATION; PROMOTER REGIONS (GENETICS); PROTEIN BINDING; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; REGULON; REPRESSOR PROTEINS; SIGNAL TRANSDUCTION; TRANSCRIPTION FACTORS; TRANSCRIPTION, GENETIC; TRISACCHARIDES;

ESCHERICHIA COLI;

EID: 35349014682     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.08.014     Document Type: Article

References (39)

1. Ade J., DeYoung B.J., Golstein C., and Innes R.W. Indirect activation of a plant nucleotide binding site-leucine-rich repeat protein by a bacterial protease. Proc. Natl. Acad. Sci. USA 104 (2007) 2531-2536
2. Ammelburg M., Frickey T., and Lupas A.N. Classification of AAA+ proteins. J. Struct. Biol. 156 (2006) 2-11
3. Bao Q., Lu W., Rabinowitz J.D., and Shi Y. Calcium blocks formation of apoptosome by preventing nucleotide exchange in Apaf-1. Mol. Cell 25 (2007) 181-192
4. Brosh Jr. R.M., and Matson S.W. Mutations in motif II of Escherichia coli DNA helicase II render the enzyme nonfunctional in both mismatch repair and excision repair with differential effects on the unwinding reaction. J. Bacteriol. 177 (1995) 5612-5621
5. Bukau B., Ehrmann M., and Boos W. Osmoregulation of the maltose regulon in Escherichia coli. J. Bacteriol. 166 (1986) 884-891
6. Danot O. A complex signaling module governs the activity of MalT, the prototype of an emerging transactivator family. Proc. Natl. Acad. Sci. USA 98 (2001) 435-440
7. Danot O., Vidal-Ingigliardi D., and Raibaud O. Two amino acid residues from the DNA-binding domain of MalT play a crucial role in transcriptional activation. J. Mol. Biol. 262 (1996) 1-11
8. Dardonville B., and Raibaud O. Characterization of malT mutants that constitutively activate the maltose regulon of Escherichia coli. J. Bacteriol. 172 (1990) 1846-1852
9. Diemand A.V., and Lupas A.N. Modeling AAA+ ring complexes from monomeric structures. J. Struct. Biol. 156 (2006) 230-243
10. Dombroski A.J., Brennan C.A., Spear P., and Platt T. Site-directed alterations in the ATP-binding domain of rho protein affect its activities as a termination factor. J. Biol. Chem. 263 (1988) 18802-18809
11. Duncan J.A., Bergstralh D.T., Wang Y., Willingham S.B., Ye Z., Zimmermann A.G., and Ting J.P. Cryopyrin/NALP3 binds ATP/dATP, is an ATPase, and requires ATP binding to mediate inflammatory signaling. Proc. Natl. Acad. Sci. USA 104 (2007) 8041-8046
12. Iyer L.M., Leipe D.D., Koonin E.V., and Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J. Struct. Biol. 146 (2004) 11-31
13. Jiang X., and Wang X. Cytochrome c promotes caspase-9 activation by inducing nucleotide binding to Apaf-1. J. Biol. Chem. 275 (2000) 31199-31203
14. Joly N., Danot O., Schlegel A., Boos W., and Richet E. The Aes protein directly controls the activity of MalT, the central transcriptional activator of the Escherichia coli maltose regulon. J. Biol. Chem. 277 (2002) 16606-16613
15. Joly N., Böhm A., Boos W., and Richet E. MalK, the ATP-binding cassette component of the Escherichia coli maltodextrin transporter, inhibits the transcriptional activator MalT by antagonizing inducer binding. J. Biol. Chem. 279 (2004) 33123-33130
16. Kim H.E., Du F., Fang M., and Wang X. Formation of apoptosome is initiated by cytochrome c-induced dATP hydrolysis and subsequent nucleotide exchange on Apaf-1. Proc. Natl. Acad. Sci. USA 102 (2005) 17545-17550
17. Larquet E., Schreiber V., Boisset N., and Richet E. Oligomeric assemblies of the Escherichia coli MalT transcriptional activator revealed by cryo-electron microcopy and image processing. J. Mol. Biol. 343 (2004) 1159-1169
18. Leipe D.D., Koonin E.V., and Aravind L. STAND, a class of P-Loop NTPases including animal and plant regulators of programmed cell death: multiple, complex domain architectures, unusual phyletic patterns, and evolution by horizontal gene transfer. J. Mol. Biol. 343 (2004) 1-28
19. Martinon F., and Tschopp J. NLRs join TLRs as innate sensors of pathogens. Trends Immunol. 26 (2005) 447-454
20. Mézard C., Davies A.A., Stasiak A., and West S.C. Biochemical properties of RuvBD113N: a mutation in helicase motif II of the RuvB hexamer affects DNA binding and ATPase activities. J. Mol. Biol. 271 (1997) 704-717
21. Moody J.E., Millen L., Binns D., Hunt J.F., and Thomas P.J. Cooperative, ATP-dependent association of the nucleotide binding cassettes during the catalytic cycle of ATP-binding cassette transporters. J. Biol. Chem. 277 (2002) 21111-21114
22. Pause A., and Sonenberg N. Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11 (1992) 2643-2654
23. Raibaud O., Vidal-Ingigliardi D., and Kolb A. Genetic studies on the promoter of malT, the gene that encodes the activator of the Escherichia coli maltose regulon. Res. Microbiol. 142 (1991) 937-942
24. Richet E., and Raibaud O. MalT, the regulatory protein of the Escherichia coli maltose system, is an ATP-dependent transcriptional activator. EMBO J. 8 (1989) 981-987
25. Richet E., Joly N., and Danot O. Two domains of MalT, the activator of the Escherichia coli maltose regulon, bear determinants essential for anti-activation by MalK. J. Mol. Biol. 347 (2005) 1-10
26. Riedl S.J., Li W., Chao Y., Schwarzenbacher R., and Shi Y. Structure of the apoptotic protease-activating factor 1 bound to ADP. Nature 434 (2005) 926-933
27. Saleh A., Srinivasula S.M., Acharya S., Fishel R., and Alnemri E.S. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J. Biol. Chem. 274 (1999) 17941-17945
28. Schlegel A., Danot O., Richet E., Ferenci T., and Boos W. The N-terminus of the Escherichia coli transcription activator MalT is the domain of interaction with MalY. J. Bacteriol. 184 (2002) 3069-3077
29. Schreiber V., and Richet E. Self-association of the Escherichia coli transcription activator MalT in the presence of maltotriose and ATP. J. Biol. Chem. 274 (1999) 33220-33226
30. Schreiber V., Steegborn C., Clausen T., Boos W., and Richet E. A new mechanism for the control of a prokaryotic transcriptional regulator: antagonistic binding of positive and negative effectors. Mol. Microbiol. 35 (2000) 765-776
31. Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., Thomas P.J., and Hunt J.F. ATP binding to the motor domain from an ABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10 (2002) 139-149
32. Steegborn C., Danot O., Huber R., and Clausen T. Crystal structure of transcription factor MalT domain III: a domain helix repeat fold implicated in regulated oligomerization. Structure 9 (2001) 1051-1060
33. Tameling W.I., Elzinga S.D., Darmin P.S., Vossen J.H., Takken F.L., Haring M.A., and Cornelissen B.J. The tomato R gene products I-2 and MI-1 are functional ATP binding proteins with ATPase activity. Plant Cell 14 (2002) 2929-2939
34. Tameling W.I., Vossen J.H., Albrecht M., Lengauer T., Berden J.A., Haring M.A., Cornelissen B.J., and Takken F.L. Mutations in the NB-ARC domain of I-2 that impair ATP hydrolysis cause autoactivation. Plant Physiol. 140 (2006) 1233-1245
35. van Duist M.M., Albrecht M., Podswiadek M., Giachino D., Lengauer T., Punzi L., and De Marchi M. A new CARD15 mutation in Blau syndrome. Eur. J. Hum. Genet. 13 (2005) 742-747
36. Vidal-Ingigliardi D., Richet E., and Raibaud O. Two MalT binding sites in direct repeat. A structural motif involved in the activation of all the promoters of the maltose regulons in Escherichia coli and Klebsiella pneumoniae. J. Mol. Biol. 218 (1991) 323-334
37. Weibezahn J., Schlieker C., Bukau B., and Mogk A. Characterization of a trap mutant of the AAA+ chaperone ClpB. J. Biol. Chem. 278 (2003) 32608-32617
38. Yan N., Xu Y., and Shi Y. 2:1 stoichiometry of the CED-4-CED-9 complex and the tetrameric CED-4: insights into the regulation of CED-3 activation. Cell Cycle 5 (2006) 31-34
39. Yu X., Acehan D., Menetret J.F., Booth C.R., Ludtke S.J., Riedl S.J., Shi Y., Wang X., and Akey C.W. A structure of the human apoptosome at 12.8 A resolution provides insights into this cell death platform. Structure 13 (2005) 1725-1735