Dae Soon Kim

Chungbuk National University

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Yong-Hee Lee

National Institute of Meteorological Sciences

Hyun Jeong Jeon

Chungbuk National University

Jae-Min Park

Chungbuk National University

Seung Ki Jung

Nutrasource

Hyun Ju Um

Chungbuk National University

Byoung Hee Park

Korea University

Hyung Jin Choi

Seoul National University

Mi Ri Jeon

Samsung Medical Center

Byung‐Chul Oh

Gachon University

Taekeun Oh

Cheongju University

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Chungbuk National University

New Generation University College

Korea University

Seoul National University

Sungkyunkwan University

Korea Research Institute of Bioscience and Biotechnology

Chungbuk National University Hospital

National University College

Seoul National University Hospital

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Differential Proteomic Analysis of Secreted Proteins from Cutinase-producing Bacillus sp. SB-007

The Plant Pathology Journal (2008)

Yeon Hee Ban Mi Ri Jeon Ji Hee Yoon Jae-Min Park Hyun Ju Um

Bacillus sp. SB-007 was isolated from pea leaves harvested from the southwestern parts of South Korea through screening on a minimal medium containing 0.2% purified cutin for its ability to induce the cutinase production. However, no cutinase was produced when it was grown in a minimal medium containing 0.2% glucose. A proteomic approach was applied to separate and characterize these differentially secreted proteins. The expression level of 83 extracellular proteins of the cutinase-producing Bacillus sp. strain SB-007 incubated in a cutinase-induced medium increased significantly as compared with that cultured in a non cutinase-induced medium containing glucose. The extracellular proteome of Bacillus sp. SB-007 includes proteins from different functional classes, such as enzymes for the degradation of various macromolecules, proteins involved in energy metabolism, sporulation, transport/binding proteins and lipoproteins, stress inducible proteins, several cellular molecule biosynthetic pathways and catabolism, and some proteins with an as yet unknown function. In addition, the two protein spots showed little similarities with the known lipolytic enzymes in the database. These secreted proteome analysis results are expected to be useful in improving the Bacillus strains for the production of industrial cutinases.

Cutinase

Proteome

Cutin

Bacillus (shape)

10.5423/ppj.2008.24.2.191

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Citations (4)

Transcription factor 7-like 2 (TCF7L2) gene polymorphism rs7903146 is associated with stroke in type 2 diabetes patients with long disease duration

Diabetes Research and Clinical Practice (2014)

Hyung Jin Choi Dong‐Hwa Lee Hyun Jeong Jeon Dae Soon Kim Yong-Hee Lee

TCF7L2

10.1016/j.diabres.2013.12.051

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Mammalian Ste20-Like Kinase and SAV1 Promote 3T3-L1 Adipocyte Differentiation by Activation of PPARγ

PLoS ONE (2012)

Byoung Hee Park Dae Soon Kim Gun Woo Won Hyun Jeong Jeon Byung‐Chul Oh

The mammalian ste20 kinase (MST) signaling pathway plays an important role in the regulation of apoptosis and cell cycle control. We sought to understand the role of MST2 kinase and Salvador homolog 1 (SAV1), a scaffolding protein that functions in the MST pathway, in adipocyte differentiation. MST2 and MST1 stimulated the binding of SAV1 to peroxisome proliferator-activated receptor γ (PPARγ), a transcription factor that plays a key role in adipogenesis. The interaction of endogenous SAV1 and PPARγ was detected in differentiating 3T3-L1 adipocytes. This binding required the kinase activity of MST2 and was mediated by the WW domains of SAV1 and the PPYY motif of PPARγ. Overexpression of MST2 and SAV1 increased PPARγ levels by stabilizing the protein, and the knockdown of SAV1 resulted in a decrease of endogenous PPARγ protein in 3T3-L1 adipocytes. During the differentiation of 3T3-L1 cells into adipocytes, MST2 and SAV1 expression began to increase at 2 days when PPARγ expression also begins to increase. MST2 and SAV1 significantly increased PPARγ transactivation, and SAV1 was shown to be required for the activation of PPARγ by rosiglitazone. Finally, differentiation of 3T3-L1 cells was augmented by MST2 and SAV1 expression and inhibited by knockdown of MST1/2 or SAV1. These results suggest that PPARγ activation by the MST signaling pathway may be a novel regulatory mechanism of adipogenesis.

10.1371/journal.pone.0030983

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Citations (28)