A Tandem of SH3-like Domains Participates in RNA Binding in KIN17, a Human Protein Activated in Response to Genotoxics

Maire, Albane le; Schiltz, M.; Stura, E.A.; Pinon‐Lataillade, Ghislaine; Couprie, Joël; Moutiez, Mireille; Gondry, Muriel; Angulo, Jaime F.; Zinn‐Justin, Sophie

doi:10.1016/j.jmb.2006.09.033

Cited by 20 publications

(18 citation statements)

References 56 publications

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“…In fact, KIN17-like proteins are found in all eukaryotes (le Maire et al, 2006), whereas SBP-domain proteins like SPL7 seem plant specific (Yamasaki et al, 2008). Furthermore, KIN17 orthologs in higher eukaryotes display a high degree of sequence similarity (Carlier et al, 2007).…”

Section: Discussionmentioning

confidence: 99%

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

2013

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Proper copper (Cu) homeostasis is required by living organisms to maintain essential cellular functions. In the model plant Arabidopsis (Arabidopsis thaliana), the SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 (SPL7) transcription factor participates in reprogramming global gene expression during Cu insufficiency in order to improve the metal uptake and prioritize its distribution to Cu proteins of major importance. As a consequence, spl7 null mutants show morphological and physiological disorders during Cu-limited growth, resulting in lower fresh weight, reduced root elongation, and chlorosis. On the other hand, the Arabidopsis KIN17 homolog belongs to a well-conserved family of essential eukaryotic nuclear proteins known to be stress activated and involved in DNA and possibly RNA metabolism in mammals. In the study presented here, we uncovered that Arabidopsis KIN17 participates in promoting the Cu deficiency response by means of a direct interaction with SPL7. Moreover, the double mutant kin17-1 spl7-2 displays an enhanced Cu-dependent phenotype involving growth arrest, oxidative stress, floral bud abortion, and pollen inviability. Taken together, the data presented here provide evidence for SPL7 and KIN17 protein interaction as a point of convergence in response to both Cu deficiency and oxidative stress.

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Section: Discussionmentioning

confidence: 99%

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

2013

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“…Tungstate, which has been previously used as a structural mimic of phosphate and thus is a marker for phosphate binding sites (32), provides an experimental constraint with which to model the position of the side chain of phosphoserine. Structural superposition of a catalytic domain of SepRS with a complex of S. cerevisiae AspRS bound to tRNA and ATP (33) indicates that the tungstate is a marker for the position of a phosphate moiety in phosphoserine rather than one of the phosphates of an ATP substrate.…”

Section: Modeling Of Phosphoseryl-adenylate In the Active Site Of Seprsmentioning

confidence: 99%

Toward understanding phosphoseryl-tRNA ^Cys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase

Kamtekar¹,

Hohn²,

Park³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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A number of archaeal organisms generate Cys-tRNA Cys in a twostep pathway, first charging phosphoserine (Sep) onto tRNA Cys and subsequently converting it to Cys-tRNA Cys . We have determined, at 3.2-Å resolution, the structure of the Methanococcus maripaludis phosphoseryl-tRNA synthetase (SepRS), which catalyzes the first step of this pathway. The structure shows that SepRS is a class II, ␣4 synthetase whose quaternary structure arrangement of subunits closely resembles that of the heterotetrameric (␣␤) 2 phenylalanyl-tRNA synthetase (PheRS). Homology modeling of a tRNA complex indicates that, in contrast to PheRS, a single monomer in the SepRS tetramer may recognize both the acceptor terminus and anticodon of a tRNA substrate. Using a complex with tungstate as a marker for the position of the phosphate moiety of Sep, we suggest that SepRS and PheRS bind their respective amino acid substrates in dissimilar orientations by using different residues.cysteine ͉ methanogen ͉ phosphoserine ͉ archaea ͉ aminoacyl-tRNA synthetase

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“…In humans, it is generally expressed at extremely low levels in all tissues and organs, except for in heart, skeletal muscle and testis [3]. Kin17 binds preferentially to the curved DNA found at hot-spots of illegitimate recombination in eukaryotic chromosomes and has a tandem SH3 domain that participates in RNA binding [4], [5]. Kin17 was determined to be a component of a multiprotein DNA replication complex and to be associated with mammalian replication origins, mRNA processing, transcription and cell cycle regulation [6], [7].…”

Section: Introductionmentioning

confidence: 99%

Up-Regulation of Kin17 Is Essential for Proliferation of Breast Cancer

Zeng

Gao²,

Yu³

et al. 2011

PLoS ONE

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BackgroundKin17 is ubiquitously expressed at low levels in human tissue and participates in DNA replication, DNA repair and cell cycle control. Breast cancer cells are characterized by enabling replicative immortality and accumulated DNA damage. However, whether kin17 contributes to breast carcinogenesis remains unknown.Methodology/Principal FindingsIn this study, we show for the first time that kin17 is an important molecule related to breast cancer. Our results show that kin17 expression was markedly increased in clinical breast tumors and was associated with tumor grade, Ki-67 expression, p53 mutation status and progesterone receptor expression, which were assessed in a clinicopathologic characteristics review. Knockdown of kin17 inhibited DNA replication and repair, blocked cell cycle progression and inhibited anchorage-independent growth, while increasing sensitivity to chemotherapy in breast cancer cells. Moreover, kin17 silencing decreased EGF-stimulated cell growth. Furthermore, overexpression of kin17 promoted DNA replication and cell proliferation in MCF-10A.Conclusions/SignificanceOur findings indicate that up-regulation of kin17 is strongly associated with cellular proliferation, DNA replication, DNA damage response and breast cancer development. The increased level of kin17 was not only a consequence of immortalization but also associated with tumorigenesis. Therefore, kin17 could be a novel therapeutic target for inhibiting cell growth in breast cancer.

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A Tandem of SH3-like Domains Participates in RNA Binding in KIN17, a Human Protein Activated in Response to Genotoxics

Cited by 20 publications

References 56 publications

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

Toward understanding phosphoseryl-tRNA ^Cys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase

Up-Regulation of Kin17 Is Essential for Proliferation of Breast Cancer

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A Tandem of SH3-like Domains Participates in RNA Binding in KIN17, a Human Protein Activated in Response to Genotoxics

Cited by 20 publications

References 56 publications

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

A Conserved KIN17 Curved DNA-Binding Domain Protein Assembles with SQUAMOSA PROMOTER-BINDING PROTEIN-LIKE7 to Adapt Arabidopsis Growth and Development to Limiting Copper Availability

Toward understanding phosphoseryl-tRNA Cys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase

Up-Regulation of Kin17 Is Essential for Proliferation of Breast Cancer

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Toward understanding phosphoseryl-tRNA ^Cys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase