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Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases.

Karpov PA, Nadezhdina ES, Yemets AI, Matusov VG, Nyporko AY, Shashina NY, Blume YB - BMC Genomics (2010)

Bottom Line: A number of SLK, MAST2 and AURKA plant homologues were identified.The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase).Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine. karpov.p.a@gmail.com

ABSTRACT
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

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Comparison of the catalytic domain spatial structures of the human protein kinase Aurora A (AURKA, STK6, PDB: 2J4Z) and the protein of unknown function STALK (S_T AURKA LIKE KINASE, UniProt: A7PY12) from V. vinifera. "a" (marked by blue) ATP-binding regions in Aurora A and STALK; "b" (marked by red) is active site; "c", "d" (marked by green) are the most spatially variable regions between the two proteins; phosphorylated Thr residues (287, 288) in the Aurora A are marked by brown. In bold are marked the only discrepancies between the corresponding functionally important residues in Aurora A versus STALK: Asn146↔Arg31, Lys141↔Arg26 in "a"; Thr288↔Thr172 in variable region "c"; Pro297↔Ala181 in the DFGWSxxxxxxxRxTxCGTxDYLPPE motif of the activating loop; Val377↔Ile263 in the D2_type destruction box - Rxx(L/I)xxVxxHPW
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Figure 9: Comparison of the catalytic domain spatial structures of the human protein kinase Aurora A (AURKA, STK6, PDB: 2J4Z) and the protein of unknown function STALK (S_T AURKA LIKE KINASE, UniProt: A7PY12) from V. vinifera. "a" (marked by blue) ATP-binding regions in Aurora A and STALK; "b" (marked by red) is active site; "c", "d" (marked by green) are the most spatially variable regions between the two proteins; phosphorylated Thr residues (287, 288) in the Aurora A are marked by brown. In bold are marked the only discrepancies between the corresponding functionally important residues in Aurora A versus STALK: Asn146↔Arg31, Lys141↔Arg26 in "a"; Thr288↔Thr172 in variable region "c"; Pro297↔Ala181 in the DFGWSxxxxxxxRxTxCGTxDYLPPE motif of the activating loop; Val377↔Ile263 in the D2_type destruction box - Rxx(L/I)xxVxxHPW

Mentions: Taking into account the critical role of Aurora kinases in microtubule protein [46] and cell division regulation [30,41,53], the plant homologue A7PY12/GSVIVT00026259001 from V. vinifera, referred herein as STALK (S_T AURKA LIKE KINASE), has been chosen for in silico spatial structure prediction (Figure 9). Sequence identity and similarity between STALK and Aurora are 60.1% and 81.7%, respectively (Table 2). In addition, identical and similar residues of STALK are distributed evenly along the whole protein chain (Figure 7), resulting in high reliability of the predicted spatial structure.


Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases.

Karpov PA, Nadezhdina ES, Yemets AI, Matusov VG, Nyporko AY, Shashina NY, Blume YB - BMC Genomics (2010)

Comparison of the catalytic domain spatial structures of the human protein kinase Aurora A (AURKA, STK6, PDB: 2J4Z) and the protein of unknown function STALK (S_T AURKA LIKE KINASE, UniProt: A7PY12) from V. vinifera. "a" (marked by blue) ATP-binding regions in Aurora A and STALK; "b" (marked by red) is active site; "c", "d" (marked by green) are the most spatially variable regions between the two proteins; phosphorylated Thr residues (287, 288) in the Aurora A are marked by brown. In bold are marked the only discrepancies between the corresponding functionally important residues in Aurora A versus STALK: Asn146↔Arg31, Lys141↔Arg26 in "a"; Thr288↔Thr172 in variable region "c"; Pro297↔Ala181 in the DFGWSxxxxxxxRxTxCGTxDYLPPE motif of the activating loop; Val377↔Ile263 in the D2_type destruction box - Rxx(L/I)xxVxxHPW
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2822528&req=5

Figure 9: Comparison of the catalytic domain spatial structures of the human protein kinase Aurora A (AURKA, STK6, PDB: 2J4Z) and the protein of unknown function STALK (S_T AURKA LIKE KINASE, UniProt: A7PY12) from V. vinifera. "a" (marked by blue) ATP-binding regions in Aurora A and STALK; "b" (marked by red) is active site; "c", "d" (marked by green) are the most spatially variable regions between the two proteins; phosphorylated Thr residues (287, 288) in the Aurora A are marked by brown. In bold are marked the only discrepancies between the corresponding functionally important residues in Aurora A versus STALK: Asn146↔Arg31, Lys141↔Arg26 in "a"; Thr288↔Thr172 in variable region "c"; Pro297↔Ala181 in the DFGWSxxxxxxxRxTxCGTxDYLPPE motif of the activating loop; Val377↔Ile263 in the D2_type destruction box - Rxx(L/I)xxVxxHPW
Mentions: Taking into account the critical role of Aurora kinases in microtubule protein [46] and cell division regulation [30,41,53], the plant homologue A7PY12/GSVIVT00026259001 from V. vinifera, referred herein as STALK (S_T AURKA LIKE KINASE), has been chosen for in silico spatial structure prediction (Figure 9). Sequence identity and similarity between STALK and Aurora are 60.1% and 81.7%, respectively (Table 2). In addition, identical and similar residues of STALK are distributed evenly along the whole protein chain (Figure 7), resulting in high reliability of the predicted spatial structure.

Bottom Line: A number of SLK, MAST2 and AURKA plant homologues were identified.The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase).Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

View Article: PubMed Central - HTML - PubMed

Affiliation: Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine. karpov.p.a@gmail.com

ABSTRACT
A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A number of SLK, MAST2 and AURKA plant homologues were identified. The closest identified homologue of human AURKA kinase was a protein of unknown function, A7PY12/GSVIVT00026259001 from Vitis vinifera (herein named as "STALK", Serine-Threonine Aurora-Like Kinase). Analysis of STALK's three-dimensional structure confirmed its relationship to the subgroup of AURKA-like protein kinases.

Show MeSH