Mammalian SMC3 C-terminal and Coiled-coil Protein Domains Specifically Bind Palindromic DNA, Do Not Block DNA Ends, and Prevent DNA Bending

Akhmedov, Alexandre T.; Gross, B.; Jessberger, Rolf

doi:10.1074/jbc.274.53.38216

Cited by 42 publications

(39 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Proteins that contain SMC-domains have been shown to participate in many aspects of higher-order chromosome organization. Like SMC proteins, MG218 is predicted to form large coiled-coils that are often involved in protein-DNA interactions (Akhmedov et al, 1999). Additional analyses are needed to determine whether DNA is present in the TO and whether MG218 protein is also involved in chromosome dynamics of M. genitalium.…”

Section: Discussionmentioning

confidence: 99%

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

et al. 2008

View full text Add to dashboard Cite

The terminal organelle is a differentiated structure that plays a key role in mycoplasma cytadherence and locomotion. For this reason, the analysis of Mycoplasma genitalium mutants displaying anomalous terminal organelles could improve our knowledge regarding the structural elements required for proper locomotion. In this study, we isolated several M. genitalium mutants having transposon insertions within the mg218 or mg317 genes, which encode the orthologues of Mycoplasma pneumoniae HMW2 and HMW3 cytoskeletal proteins, respectively. As expected, mg218 " and mg317 " mutants exhibit a reduced gliding motility, although their ability to attach to solid surfaces was not completely abolished. Interestingly, most of the mg218 " mutants expressed N-terminal MG218 derivatives and showed the presence of short terminal organelles retaining many of the functions displayed by this structure in the wild-type strain, suggesting that the N-terminal region of this protein is an essential element in the architecture of the terminal organelle. Separately, the analysis of mg317 " mutants indicates that MG317 protein is involved in the formation of the terminal button and contributes to anchoring the electron-dense core to the cell membrane. The results presented here clearly show that MG218 and MG317 proteins are implicated in the maintenance of gliding motility and cytadherence in M. genitalium.

show abstract

Section: Discussionmentioning

confidence: 99%

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

et al. 2008

View full text Add to dashboard Cite

show abstract

“…4). For both dimers, a 232-bp pUC19 plasmid DNA fragment (27,28) that lacks repetitive or palindromic sequences serves as a comparatively weak competitor (50% competition at approximately 315 pg (2.1 fmol) of competitor DNA for SMC1␣/SMC3 and little competition with up to 450 pg (2.9 fmol) of competitor for SMC1␤/SMC3) (Fig. 4A).…”

Section: Purification and Dimerization Of Smc1/smc3mentioning

confidence: 99%

“…4A). In contrast, a 230-bp M13 dsDNA fragment (27,28) that has palindromic sequences with a potentially very high stability of stem-loop structures effectively competes (approximately 50% competition for SMC1␣/SMC3 at 20 pg (0.1 fmol of competitor) and for SMC1␤/SMC3 at 90 pg (0.6 fmol of competitor)) (Fig. 4B).…”

Section: Purification and Dimerization Of Smc1/smc3mentioning

confidence: 99%

“…Earlier, it has been shown that individual C-terminal domains of a variety of SMC proteins, the RC-1 complex, the SMC1/3 heterodimer, or a prokaryotic homodimer promote reannealing of complementary strands of DNA (15,27,28,41,42). Reannealing of DNA single strands is thought to reflect the potential of proteins or other agents to stabilize the double-stranded form or to help in annealing of a DNA strand to a homolog in DNA recombination.…”

Section: Purification and Dimerization Of Smc1/smc3mentioning

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).…”

mentioning

confidence: 99%

See 2 more Smart Citations

DNA Interaction and Dimerization of Eukaryotic SMC Hinge Domains

Chiu

Revenkova

Jessberger

2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

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...

show abstract

Emerging roles of RB family: New defense mechanisms against tumor progression

Indovina

Marcelli

Casini

et al. 2012

Journal Cellular Physiology

View full text Add to dashboard Cite

The retinoblastoma (RB) family of proteins, including RB1/p105, retinoblastoma-like 1 (RBL1/p107), and retinoblastoma-like 2 (RBL2/p130), is principally known for its central role on cell cycle regulation. The inactivation of RB proteins confers a growth advantage and underlies multiple types of tumors. Recently, it has been shown that RB proteins have other important roles, such as preservation of chromosomal stability, induction and maintenance of senescence and regulation of apoptosis, cellular differentiation, and angiogenesis. RB proteins are involved in many cellular pathways and act as transcriptional regulators able to bind several transcription factors, thus antagonizing or potentiating their functions. Furthermore, RB proteins might control the expression of specific target genes by recruiting chromatin remodeling enzymes. Although many efforts have been made to dissect the different functions of RB proteins, it remains still unclear which are necessary for cancer suppression and the role they play at distinct steps of carcinogenesis. Moreover, RB proteins can behave differently in various cell types or cell states. Elucidating the intricate RB protein network in regulating cell fate might provide the knowledge necessary to explain their potent tumor suppressor activity and to design novel therapeutic strategies.

show abstract

Mammalian SMC3 C-terminal and Coiled-coil Protein Domains Specifically Bind Palindromic DNA, Do Not Block DNA Ends, and Prevent DNA Bending

Cited by 42 publications

References 39 publications

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

Role of Mycoplasma genitalium MG218 and MG317 cytoskeletal proteins in terminal organelle organization, gliding motility and cytadherence

DNA Interaction and Dimerization of Eukaryotic SMC Hinge Domains

Emerging roles of RB family: New defense mechanisms against tumor progression

Contact Info

Product

Resources

About