Limits...
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.

Show MeSH
Alignment of human Aurora A and its plant homologues. NP_BIND (ATP) - nucleotide phosphate binding site; Binding site (ATP) - ATP binding site; ACT_SITE - proton acceptor site
© Copyright Policy - open-access
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC2822528&req=5

Figure 7: Alignment of human Aurora A and its plant homologues. NP_BIND (ATP) - nucleotide phosphate binding site; Binding site (ATP) - ATP binding site; ACT_SITE - proton acceptor site

Mentions: In an earlier paper on plant homologues of Aurora kinases [52], the authors described a high level of identity for Aurora catalytic domains from Arabidopsis (64-95%). We now report additional homologues belonging to O. sativa ssp. japonica (Q5SNH4/Os01g0191800, Q4R1K7/OsAUR1), O. sativa ssp. indica (A2WLL4/OsI_00731), P. balsamifera ssp. trichocarpa (A9PFI9/POPTRDRAFT_819526), V. vinifera (A7P4F7/GSVIVT00032134001, A5BPE0/VITISV_023325, A7PY12/GSVIVT00026259001), Zea mays (B4F8A1/LOC100191291) and A. thaliana (AUR2 Isof. 1 and AUR2 Isof. 2 (At2g25880), AUR1/At4g32830, AUR3/At2g45490). Together with a low gap percentage (1-2%), such a high identity reflects not only sequence homology but also homology of structure and function (Figure 7). As evident from the annotations in the Swiss-Prot database kinases AUR1/At4g32830, AUR2 Isof. 1 and AUR2 Isof. 2 (At2g25880) and AUR3/At2g45490 from A. thaliana could be functional homologues. Sequence Q4R1K7/OsAUR1 from O. sativa ssp. japonica in the TrEMBL database [53] is also annotated as a potential plant Aurora kinase.


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)

Alignment of human Aurora A and its plant homologues. NP_BIND (ATP) - nucleotide phosphate binding site; Binding site (ATP) - ATP binding site; ACT_SITE - proton acceptor site
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 7: Alignment of human Aurora A and its plant homologues. NP_BIND (ATP) - nucleotide phosphate binding site; Binding site (ATP) - ATP binding site; ACT_SITE - proton acceptor site
Mentions: In an earlier paper on plant homologues of Aurora kinases [52], the authors described a high level of identity for Aurora catalytic domains from Arabidopsis (64-95%). We now report additional homologues belonging to O. sativa ssp. japonica (Q5SNH4/Os01g0191800, Q4R1K7/OsAUR1), O. sativa ssp. indica (A2WLL4/OsI_00731), P. balsamifera ssp. trichocarpa (A9PFI9/POPTRDRAFT_819526), V. vinifera (A7P4F7/GSVIVT00032134001, A5BPE0/VITISV_023325, A7PY12/GSVIVT00026259001), Zea mays (B4F8A1/LOC100191291) and A. thaliana (AUR2 Isof. 1 and AUR2 Isof. 2 (At2g25880), AUR1/At4g32830, AUR3/At2g45490). Together with a low gap percentage (1-2%), such a high identity reflects not only sequence homology but also homology of structure and function (Figure 7). As evident from the annotations in the Swiss-Prot database kinases AUR1/At4g32830, AUR2 Isof. 1 and AUR2 Isof. 2 (At2g25880) and AUR3/At2g45490 from A. thaliana could be functional homologues. Sequence Q4R1K7/OsAUR1 from O. sativa ssp. japonica in the TrEMBL database [53] is also annotated as a potential plant Aurora kinase.

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