RIO1, an extraordinary novel protein kinase.

by: M Angermayr, W Bandlow

FEBS Lett, Vol. 524, No. 1-3. (31 July 2002), pp. 31-36.

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Abstract

RIO1 and Rio-related proteins display little similarity of primary sequence with conventional protein kinases. Based on secondary structure alignments, we show that it contains the domain structure (subdomains I-XI) and conserved secondary structure elements found in conventional protein kinases. We show that recombinant wild-type Rio1p isolated from Escherichia coli displays kinase activity which depends on autophosphorylation and magnesium or manganese as ATP-activating ions. An initial biochemical characterization of Rio1p is presented.

@article{citeulike:2193611, abstract = {RIO1 and Rio-related proteins display little similarity of primary sequence with conventional protein kinases. Based on secondary structure alignments, we show that it contains the domain structure (subdomains I-XI) and conserved secondary structure elements found in conventional protein kinases. We show that recombinant wild-type Rio1p isolated from Escherichia coli displays kinase activity which depends on autophosphorylation and magnesium or manganese as ATP-activating ions. An initial biochemical characterization of Rio1p is presented.}, address = {Department Biologie I, Bereich Genetik, Ludwig-Maximilians-Universit\"{a}t M\"{u}nchen, Maria-Ward-Strasse 1a, D-80638 Munich, Germany. M.Angermayr@lrz.uni-muenchen.de}, author = {Angermayr, M. and Bandlow, W. }, citeulike-article-id = {2193611}, issn = {0014-5793}, journal = {FEBS Lett}, keywords = {alignment, domain, kinase, rio}, month = {July}, number = {1-3}, pages = {31--36}, posted-at = {2008-01-04 07:05:31}, priority = {2}, title = {RIO1, an extraordinary novel protein kinase.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12135737}, volume = {524}, year = {2002} }

RIS record

TY - JOUR ID - citeulike:2193611 L3 - citeulike-article-id:2193611 TI - RIO1, an extraordinary novel protein kinase. JF - FEBS Lett VL - 524 IS - 1-3 SP - 31 EP - 36 AD - Department Biologie I, Bereich Genetik, Ludwig-Maximilians-Universität München, Maria-Ward-Strasse 1a, D-80638 Munich, Germany. M.Angermayr@lrz.uni-muenchen.de SN - 0014-5793 N2 - RIO1 and Rio-related proteins display little similarity of primary sequence with conventional protein kinases. Based on secondary structure alignments, we show that it contains the domain structure (subdomains I-XI) and conserved secondary structure elements found in conventional protein kinases. We show that recombinant wild-type Rio1p isolated from Escherichia coli displays kinase activity which depends on autophosphorylation and magnesium or manganese as ATP-activating ions. An initial biochemical characterization of Rio1p is presented. KW - alignment KW - domain KW - kinase KW - rio AU - Angermayr, M AU - Bandlow, W PY - 2002/07/31/ UR - http://view.ncbi.nlm.nih.gov/pubmed/12135737 ER -

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