title: Possible Roles of LAMMER Kinase Lkh1 in Fission Yeast by Comparative Proteome Analysis.
abstract: To investigate the possible roles of LAMMER kinase homologue, Lkh1, in Schizosaccharomyces pombe, whole proteins were extracted from wild type and lkh1-deletion mutant cells and subjected to polyacrylamide gel electrophoresis. Differentially expressed proteins were identified by tandem mass spectrometry (MS/MS) and were compared with a protein database. In whole-cell extracts, 10 proteins were up-regulated and 9 proteins were down-regulated in the mutant. In extracellular preparations, 6 proteins were up-regulated in the lkh1 (+) null mutant and 4 proteins successfully identified: glycolipid anchored surface precursor, β-glucosidase (Psu1), cell surface protein, glucan 1,3-β-glucosidase (Bgl2), and exo-1,3 β-glucanase (Exg1). These results suggest that Lkh1 is involved in regulating cell wall assembly.
authors: BioRefinery Center, Korea Research Institute of Chemical Technology, Daejeon 305-600, Korea.
authors: Soo-Jin
authors: SJ
authors: Cho
authors: Young Hwan
authors: YH
authors: Kim
authors: Hee-Moon
authors: HM
authors: Park
authors: Kwang-Soo
authors: KS
authors: Shin
keywords: Lkh1; Proteome analyses; Schizosaccharomyces pombe
references: Proteomics. 2006 May;6(9):2772-96
references: 16548067
references: Antonie Van Leeuwenhoek. 1990 Oct;58(3):137-46
references: 2256672
references: Biochem Biophys Res Commun. 2003 Nov 28;311(4):1078-83
references: 14623292
references: FEMS Microbiol Rev. 2002 Aug;26(3):239-56
references: 12165426
references: J Bacteriol. 1998 Oct;180(19):5030-7
references: 9748433
references: Mol Gen Genet. 1994 Mar;242(6):641-8
references: 8152414
references: EMBO J. 1994 Dec 15;13(24):6099-106
references: 7813446
references: J Bacteriol. 1993 Apr;175(7):2102-6
references: 8458852
references: Arch Med Res. 1993 Autumn;24(3):293-9
references: 8298280
references: Biochemistry. 1978 Nov 14;17(23):4900-7
references: 363146
references: Trends Cell Biol. 1995 May;5(5):207-12
references: 14731451
references: EMBO J. 2003 Dec 1;22(23):6256-66
references: 14633985
references: Biochem Biophys Res Commun. 1999 Aug 27;262(2):368-74
references: 10462482
references: Biol Bull. 2003 Dec;205(3):276-84
references: 14672982
references: FEBS Lett. 2007 Jul 24;581(18):3473-8
references: 17612531
references: Biochem Biophys Res Commun. 2001 Dec 21;289(5):1237-42
references: 11741326
references: Methods Enzymol. 1991;194:795-823
references: 2005825
references: Mol Biol Cell. 1998 Nov;9(11):3071-83
references: 9802897
references: J Bacteriol. 1989 Nov;171(11):6259-64
references: 2509432
references: Mol Biol Cell. 2000 Aug;11(8):2631-42
references: 10930459
references: Microbiol Rev. 1993 Jun;57(2):402-14
references: 8336673
references: Proteomics. 2002 Sep;2(9):1325-46
references: 12362351
references: J Biol Chem. 2010 Apr 30;285(18):13797-806
references: 20200159