Structural Maintenance of Chromosomes Protein C-terminal Domains Bind Preferentially to DNA with Secondary Structure

Akhmedov, Alexandre T.; Frei, C.; Tsai-Pflugfelder, Monika; Kemper, Börries; Gasser, Susan M.; Jessberger, Rolf

doi:10.1074/jbc.273.37.24088

Cited by 99 publications

(97 citation statements)

References 45 publications

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“…Tool, two previously characterized domains (SMC_ prok_B and SMC_N) containing long coiled-coil regions for protein interaction were identified in TNO1 (Akhmedov et al, 1998;Geer et al, 2002). Although SMC domains are commonly found in structural maintenance of chromosome proteins, they are also found in other proteins with multiple coiled-coil domains, such as vesicle-tethering factors and cytoskeletonbinding proteins.…”

Section: Identity Of Tno1mentioning

confidence: 99%

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Kim

Bassham

2011

Plant Physiology

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The Arabidopsis (Arabidopsis thaliana) soluble N-ethylmaleimide-sensitive factor attachment protein receptor SYP41 is involved in vesicle fusion at the trans-Golgi network (TGN) and interacts with AtVPS45, SYP61, and VTI12. These proteins are involved in diverse cellular processes, including vacuole biogenesis and stress tolerance. A previously uncharacterized protein, named TNO1 (for TGN-localized SYP41-interacting protein), was identified by coimmunoprecipitation as a SYP41-interacting protein.TNO1 was found to localize to the TGN by immunofluorescence microscopy. A tno1 mutant showed increased sensitivity to high concentrations of NaCl, KCl, and LiCl and also to mannitol-induced osmotic stress. Localization of SYP61, which is involved in the salt stress response, was disrupted in the tno1 mutant. Vacuolar proteins were partially secreted to the apoplast in the tno1 mutant, suggesting that TNO1 is required for efficient protein trafficking to the vacuole. The tno1 mutant had delayed formation of the brefeldin A (BFA) compartment in cotyledons upon application of BFA, suggesting less efficient membrane fusion processes in the mutant. Unlike most TGN proteins, TNO1 does not relocate to the BFA compartment upon BFA treatment. These data demonstrate that TNO1 is involved in vacuolar trafficking and salt tolerance, potentially via roles in vesicle fusion and in maintaining TGN structure or identity.

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Section: Identity Of Tno1mentioning

confidence: 99%

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Kim

Bassham

2011

Plant Physiology

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“…Structural maintenance of chromosomes 1 (SMC1) contains two long coiled-coil domains separated by a short hinge region and an ATP-/GTP-binding domain (Strunnikov and Jessberger, 1999). These proteins have been shown to bind DNA and likely play a role in sister chromatid cohesion and DNA recombination (Akhmedov et al, 1998).…”

Section: Pmi2 Structure and Functionmentioning

confidence: 99%

Plastid Movement Impaired 2, a New Gene Involved in Normal Blue-Light-Induced Chloroplast Movements in Arabidopsis

2006

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Chloroplasts move in a light-dependent manner that can modulate the photosynthetic potential of plant cells. Identification of genes required for light-induced chloroplast movement is beginning to define the molecular machinery that controls these movements. In this work, we describe plastid movement impaired 2 (pmi2), a mutant in Arabidopsis (Arabidopsis thaliana) that displays attenuated chloroplast movements under intermediate and high light intensities while maintaining a normal movement response under low light intensities. In wild-type plants, fluence rates below 20 mmol m 22 s 21 of blue light lead to chloroplast accumulation on the periclinal cell walls, whereas light intensities over 20 mmol m 22 s 21 caused chloroplasts to move toward the anticlinal cell walls (avoidance response). However, at light intensities below 75 mmol m 22 s 21 , chloroplasts in pmi2 leaves move to the periclinal walls; 100 mmol m 22 s 21 of blue light is required for chloroplasts in pmi2 to move to the anticlinal cell walls, indicating a shift in the light threshold for the avoidance response in the mutant. The pmi2 mutation has been mapped to a gene that encodes a protein of unknown function with a large coiled-coil domain in the N terminus and a putative P loop. PMI2 shares sequence and structural similarity with PMI15, another unknown protein in Arabidopsis that, when mutated, causes a defect in chloroplast avoidance under high-light intensities.

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“…Electrophoresis Mobility Shift Assay-These assays were performed as described earlier (19,27). Briefly, 30-l reaction mixtures containing 0.5-1 ng (3000 -6000 cpm) of 32 P 5Ј-labeled DNA in 20 mM HEPES, pH 7.5, 1 mM dithiothreitol, 100 g/ml bovine serum albumin, and protein as indicated.…”

Section: Fig 2 Purification Of Smc Hinge Domainsmentioning

confidence: 99%

“…However, SMC proteins are known to bind DNA, at least in vitro. Individual C-terminal but not N-terminal domains from a variety of yeast and higher eukaryotic SMC proteins, and one coiled-coil region from mammalian SMC3, were found to bind DNA, preferentially doublestranded (ds) 1 substrates that contain palindromic sequences, potentially form stem-loop structures, or are A/T-rich (27,28).…”

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confidence: 99%

DNA Interaction and Dimerization of Eukaryotic SMC Hinge Domains

Chiu

Revenkova

Jessberger

2004

Journal of Biological Chemistry

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The eukaryotic SMC1/SMC3 heterodimer is essential for sister chromatid cohesion and acts in DNA repair and recombination. Dimerization depends on the central hinge domain present in all SMC proteins, which is flanked at each side by extended coiled-coil regions that terminate in specific globular domains. Here we report on DNA interactions of the eukaryotic, heterodimeric SMC1/SMC3 hinge regions, using the two known isoforms, SMC1␣/SMC3 and the meiotic SMC1␤/SMC3. Both dimers bind DNA with a preference for double-stranded DNA and DNA rich in potential secondary structures. Both dimers form large protein-DNA networks and promote reannealing of complementary DNA strands. DNA binding but not dimerization depends on approximately 20 amino acids of transitional sequence into the coiledcoil region. Replacement of three highly conserved glycine residues, thought to be required for dimerization, in one of the two hinge domains still allows formation of a stable dimer, but if two hinge domains are mutated dimerization fails. Single-mutant dimers bind DNA, but hinge monomers do not. Together, we show that eukaryotic hinge dimerization does not require conserved glycines in both hinge domains, that only the transition into the coiled-coil region rather than the entire coiledcoil region is necessary for DNA binding, and that dimerization is required but not sufficient for DNA binding of the eukaryotic hinge heterodimer.Eukaryotic SMC (structural maintenance of chromosomes) proteins are essential for sister chromatid cohesion and proper chromosome condensation and also act in response to DNA damage, in DNA recombination and repair, and in gene dosage compensation (for recent reviews see Refs. 1-6).SMC proteins, which are between 120 and 160 kDa in molecular mass, feature a design reminiscent of motor proteins. The C-terminal and N-terminal globular domains are separated by extended coiled-coil regions and a hinge domain at the center. Six members of the eukaryotic SMC protein family are known, named SMC1-SMC6 for most eukaryotic organisms. They form three types of heterodimers: SMC1/SMC3, SMC2/SMC4, and SMC5/SMC6. One heterodimer each constitutes a core component of a larger multiprotein complex that acts in one of the key functions described for SMC proteins. The best described complexes are cohesin (7-9), which is based on SMC1/SMC3, and condensin with its SMC2/SMC4 core (10, 11). The SMC5/SMC6 heterodimer forms a multiprotein complex that acts in postreplicative recombinational repair of DNA damage (12, 13). Also, there are several other complexes such as a mammalian complex called RC-1, which has been implicated in DNA recombination and repair reactions (14, 15), a DNA damage response-dependent complex that forms upon phosphorylation of SMC1 (16, 17), and a gene dosage compensation complex in Caenorhabditis elegans that contains SMC2 and SMC4 homologs and is responsible for maintaining the same level of X chromosome expression in XX and XO animals (18). In meiotic cells, there exist at least two, probably more, meiosis-s...

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Structural Maintenance of Chromosomes Protein C-terminal Domains Bind Preferentially to DNA with Secondary Structure

Cited by 99 publications

References 45 publications

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

TNO1 Is Involved in Salt Tolerance and Vacuolar Trafficking in Arabidopsis

Plastid Movement Impaired 2, a New Gene Involved in Normal Blue-Light-Induced Chloroplast Movements in Arabidopsis

DNA Interaction and Dimerization of Eukaryotic SMC Hinge Domains

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