Side-chain effects on peptidyl-prolyl cis/trans isomerisation

Reimer, Ulf; Scherer, Gerd; Drewello, Mario; Kruber, S.; Schutkowski, Mike; Fischer, Gunter

doi:10.1006/jmbi.1998.1770

Cited by 344 publications

(462 citation statements)

References 58 publications

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“…4b and Supplementary Table 2). We interpret the slow-folding species as an in vitro folding artifact caused by the cis-to-trans isomerization of non-native cis-prolyl peptide bonds that accumulate in FimA U ox upon longterm incubation in denaturant; as the only two prolyl peptide bonds (isoleucine-proline and threonine-proline) in FimA are in the trans conformation in the native state 28 , 20% of FimA U ox molecules with at least one non-native cis-prolyl peptide bond is indeed predicted for unfolded FimA on the basis of studies on unstructured model peptides 33 . In addition, the slower phase in Figure 4b shows a concentration-independent half-life of 18 s (Supplementary Table 2), which is in the typical range for a prolyl cis-to-trans isomerization at 25 °C 34 .…”

Section: Kinetics Of Dsba-and Fimc-catalyzed Fima Foldingmentioning

confidence: 99%

Quality control of disulfide bond formation in pilus subunits by the chaperone FimC

et al. 2012

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Section: Kinetics Of Dsba-and Fimc-catalyzed Fima Foldingmentioning

confidence: 99%

Quality control of disulfide bond formation in pilus subunits by the chaperone FimC

et al. 2012

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“…For the two tandem proline residues specific to the conformation of the Trp 104 -Pro 105 and Pro 105 -Pro 106 motifs, four conformers in the solution were predicted 35 ARTICLE peaks from the minor conformers in the ROESY spectra ( Supplementary Fig. 8), it is technically impossible for the signal assignment and difficult to calculate the rate constants of the minor conformers.…”

Section: Lrt2 Catalyses Cis/trans Isomerization Of Osiaa11 Peptidementioning

confidence: 99%

“…8), it is technically impossible for the signal assignment and difficult to calculate the rate constants of the minor conformers. Considering the lowest cis population of Xaa-Pro bond, where Xaa as a proline 35 and the type II helix with trans conformation dominating the poly-Pro sequence, the two major conformers of OsIAA11 peptide were deduced as T 105 T 106 and C 105 T 106 , while the minor conformers were predicted as T 105 C 106 and C 105 C 106 (Fig. 2d).…”

Section: Lrt2 Catalyses Cis/trans Isomerization Of Osiaa11 Peptidementioning

confidence: 99%

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

et al. 2015

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In plants, auxin signalling is initiated by the auxin-promoted interaction between the auxin receptor TIR1, an E3 ubiquitin ligase, and the Aux/IAA transcriptional repressors, which are subsequently degraded by the proteasome. Gain-of-function mutations in the highly conserved domain II of Aux/IAAs abolish the TIR1-Aux/IAA interaction and thus cause an auxin-resistant phenotype. Here we show that peptidyl-prolyl isomerization of rice OsIAA11 catalysed by LATERAL ROOTLESS2 (LRT2), a cyclophilin-type peptidyl-prolyl cis/trans isomerase, directly regulates the stability of OsIAA11. NMR spectroscopy reveals that LRT2 efficiently catalyses the cis/trans isomerization of OsIAA11. The lrt2 mutation reduces OsTIR1-OsIAA11 interaction and consequently causes the accumulation of a higher level of OsIAA11 protein. Moreover, knockdown of the OsIAA11 expression partially rescues the lrt2 mutant phenotype in lateral root development. Together, these results illustrate cyclophilincatalysed peptidyl-prolyl isomerization promotes Aux/IAA degradation, as a mechanism regulating auxin signalling.

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“…The trans form of the bond is generally slightly lower in energy and, thus, is the preferred orientation. The percentage of peptide bonds in the cis conformation can vary between 6.0 and 37.7% in disordered peptides depending on the identity of the residue preceding the proline (59). In folded proteins the percentage of bonds in the cis conformation ranges from 1.8 to 12.4% because a single conformation is usually adopted that restricts the bond to one or the other isomer.…”

Section: Analysis Of Mh2-interactingmentioning

confidence: 99%

Disorder in a Target for the Smad2 Mad Homology 2 Domain and Its Implications for Binding and Specificity

Chong

Ozdamar

Wrana

et al. 2004

Journal of Biological Chemistry

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The Smad2 Mad homology 2 (MH2) domain binds to a diverse group of proteins which do not share a common sequence motif. We have used NMR to investigate the structure of one of these interacting proteins, the Smad binding domain (SBD) of Smad anchor for receptor activation (SARA). Our results indicate that the unbound SBD is highly disordered and forms no stable secondary or tertiary structures. Additionally we have used fluorescence binding studies to study the interaction between the MH2 domain and SBD and find that no region of the SBD dominates the interaction between the MH2 and the SBD. Our results are consistent with a series of hydrophobic patches on the MH2 that are able to recognize disordered regions of proteins. These findings elucidate a mechanism by which a single domain (MH2) can specifically recognize a diverse set of proteins which are unrelated by sequence, lead to a clearer picture of how MH2 domains function in the transforming growth factor-␤-signaling pathway and suggest possible mechanisms for controlling interactions with MH2 domains.The TGF-␤ 1 superfamily of cytokines plays an essential role in a variety of cellular responses including differentiation, cell fate specification, and growth inhibition (1-4). Dysregulation of TGF-␤ signaling has been associated with many diseases, such as human cancers, fibrosis, hereditary hemorrhagic telangiectasia (2, 5), and Marfan syndrome (6). TGF-␤ signal transduction is mediated intracellularly by the Smad proteins, including the R-Smads (receptor-regulated Smads), the I-Smads (inhibitor Smads), and the Co-Smad (common Smad). Ligand binding to the TGF-␤ receptor complex or a homologous complex leads to receptor phosphorylation of the R-Smads (7, 8). Subsequently, the phosphorylated R-Smads can interact with the Co-Smad, Smad4, and accumulate in the nucleus (9, 10). In the nucleus the Smad proteins bind to transcription factors and promoter regions and play a role in the transcription of various genes (11, 12).The R-Smads and Smad4 consist of a conserved N-terminal Mad homology 1 (MH1) domain and a conserved C-terminal MH2 domain joined by a poorly conserved linker region. The MH1 domain is known to function in binding DNA (13). The MH2 domain appears to exhibit many different roles and binds to many different proteins. Although many modular protein domains involved in signal transduction, such as SH3, SH2, WW, PTB, and PDZ domains, interact with a recognizable sequence motif (14), MH2 domains appear to be able to bind to a wide variety of ligands that do not share a single common motif. For example the MH2 domain of Smad2 binds a plethora of non-homologous proteins including SARA (15), the TGF-␤ receptors, FoxH1 (16), Mixer (17), TGIF (18,19), CBP (20), AML1 (21,22), Ski (23,24), and SIP1 (25). These interacting partners represent a diverse group of protein types, encompassing receptors, membrane anchoring proteins, and transcription factors. Furthermore, they have no region of sequence or structural similarity in common. A key question is how the M...

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Side-chain effects on peptidyl-prolyl cis/trans isomerisation

Cited by 344 publications

References 58 publications

Quality control of disulfide bond formation in pilus subunits by the chaperone FimC

Quality control of disulfide bond formation in pilus subunits by the chaperone FimC

Peptidyl-prolyl isomerization targets rice Aux/IAAs for proteasomal degradation during auxin signalling

Disorder in a Target for the Smad2 Mad Homology 2 Domain and Its Implications for Binding and Specificity

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