Structure of the Carboxypeptidase Y Inhibitor IC in Complex with the Cognate Proteinase Reveals a Novel Mode of the Proteinase–Protein Inhibitor Interaction

Mima, Joji; Hayashida, Minoru; Fujii, Tomomi; Narita, Yusuke; Ueda, Mitsuyoshi; Hata, Yasuo

doi:10.1016/j.jmb.2004.12.051

Cited by 35 publications

(58 citation statements)

References 39 publications

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“…However, the molecular functions of PEBPs are largely unknown. PEBPs have been reported to function as Raf-1 kinase inhibitor proteins in mammalians and as Ser protease inhibitors in yeast (Yeung et al, 1999;Mima et al, 2005). Here, we demonstrated that one PEBP, TFL1, is involved in transcriptional repression.…”

Section: Discussionmentioning

confidence: 64%

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

2011

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TERMINAL FLOWER1 (TFL1) is a key regulator of flowering time and the development of the inflorescence meristem in Arabidopsis thaliana. TFL1 and FLOWERING LOCUS T (FT) have highly conserved amino acid sequences but opposite functions. For example, FT promotes flowering and TFL1 represses it; FT-overexpressing plants and TFL1 loss-of-function mutants have a similar phenotype production of terminal flowers in the shoot apex. FT is believed to function in a transcriptional activator complex by interacting with FD. Here, we demonstrate that TFL1 is involved in the transcriptional repression of genes that are activated by FT. We analyzed transgenic plants overexpressing TFL1 fused to a transcriptional repressor domain (TFL1-SRDX) or an activator domain (TFL1-VP16). Plants carrying 35S:TFL1-SRDX showed delayed flowering similar to 35S:TFL1 plants, and plants carrying 35S:TFL1-VP16 showed an early flowering phenotype and produced terminal flowers. Furthermore, the tfl1 and 35S:TFL1-VP16 plant phenotypes were strongly suppressed by the fd mutation, and TFL1 interacted with FD in the cell nucleus, as shown by bimolecular fluorescence complementation experiments. We conclude that TFL1 negatively modulates the FD-dependent transcription of target genes to fine-tune flowering time and the development of the inflorescence meristem.

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Section: Discussionmentioning

confidence: 64%

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

2011

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“…It has also been reported that mCPY was specifically inhibited by I C , a proteinous proteinase inhibitor in the yeast S. cerevisiae. 13,15) Hence, to explore the similarity in inhibitory functions between the propeptide of proCPY and I C , amino acid sequence alignment between proCPY and I C was done (Fig. 2A).…”

Section: Resultsmentioning

confidence: 99%

“…2B). The N-terminal inhibitory reactive site, which is essential both for the inhibitory function toward mCPY and for the complex formation with mCPY, interacts with the S1 substrate binding site of mCPY, and the secondary CPY-binding site interacts with the hydrophobic surface flanked by the mCPY active site 13) (Fig. 1A).…”

Section: Resultsmentioning

confidence: 99%

“…This is the first report to the effect that a proCPY propeptide and its endogenous inhibitor (I C ) show sequence similarity, unlike the subtilisin propeptide and its foreign inhibitors. As the N-terminus of I C bound directly to the substrate-binding site of mCPY and inhibited its activity, 13) the C-terminus of the propeptide, which is similar to the partial sequence of I C , might also bind to the substrate-binding site and keep the CPY in inactive form. It has been reported that the maturation of CPY is processed by four-step digestion of the propeptide (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…In particular, the N-terminal inhibitory reactive site is essential for CPY inhibition, because the N-terminal (Met1-Phe7) deleted mutant of I C does not form a complex with mCPY and has no inhibitory activity toward mCPY. 13) I C has a homologous protein, I C h, which has no CPY inhibitory activity. 14) This is because I C h lacks the N-terminal seven amino acids present in I C .…”

Section: )mentioning

confidence: 99%

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Identification of Interaction Site of Propeptide toward Mature Carboxypeptidase Y (mCPY) Based on the Similarity between Propeptide and CPY Inhibitor (I^C)

Nagayama

Kuroda

Ueda

2012

Bioscience, Biotechnology, and Biochemistry

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NMR structure of a phosphatidyl‐ethanolamine binding protein from Drosophila

Rautureau¹,

Vovelle²,

Schoentgen³

et al. 2010

Proteins

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Structure of the Carboxypeptidase Y Inhibitor IC in Complex with the Cognate Proteinase Reveals a Novel Mode of the Proteinase–Protein Inhibitor Interaction

Cited by 35 publications

References 39 publications

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

Identification of Interaction Site of Propeptide toward Mature Carboxypeptidase Y (mCPY) Based on the Similarity between Propeptide and CPY Inhibitor (I^C)

NMR structure of a phosphatidyl‐ethanolamine binding protein from Drosophila

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Structure of the Carboxypeptidase Y Inhibitor IC in Complex with the Cognate Proteinase Reveals a Novel Mode of the Proteinase–Protein Inhibitor Interaction

Cited by 35 publications

References 39 publications

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

ArabidopsisTERMINAL FLOWER1 Is Involved in the Regulation of Flowering Time and Inflorescence Development through Transcriptional Repression

Identification of Interaction Site of Propeptide toward Mature Carboxypeptidase Y (mCPY) Based on the Similarity between Propeptide and CPY Inhibitor (IC)

NMR structure of a phosphatidyl‐ethanolamine binding protein from Drosophila

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Identification of Interaction Site of Propeptide toward Mature Carboxypeptidase Y (mCPY) Based on the Similarity between Propeptide and CPY Inhibitor (I^C)