DNA binding protein from ovaries of the frog, Xenopus laevis which promotes concatenation of linear DNA

Bayne, Marvin L.; Alexander, Robert F.; Benbow, Robert M.

doi:10.1016/0022-2836(84)90416-9

Cited by 24 publications

(8 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In X. laevis, protein synthesis is required for the initiation of maturation and for progression to meiosis 11 (22,44). Translation of factors regulating the activity of maturation-promoting factor, which initiates egg maturation, has been shown to occur in this cycloheximide-sensitive period (9,20,22,30,44 (2,10,15,48), joining is detectable only in mature eggs about 10 h after GVBD (Fig. 4).…”

Section: Resultsmentioning

confidence: 96%

Activation of a system for the joining of nonhomologous DNA ends during Xenopus egg maturation.

1992

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 96%

Activation of a system for the joining of nonhomologous DNA ends during Xenopus egg maturation.

1992

View full text Add to dashboard Cite

show abstract

“…DNA concentrations are expressed as nucleotide equivalents. The assay for retention of double-stranded DNA on nitrocellulose filters through binding to protein (filter binding assay) was performed essentially as described elsewhere (3).…”

Section: Methodsmentioning

confidence: 99%

Novel Meiosis-Specific Isoform of Mammalian SMC1

Revenkova

Eijpe

Heyting

et al. 2001

Molecular and Cellular Biology

194

217

View full text Add to dashboard Cite

Structural maintenance of chromosomes (SMC) proteins fulfill pivotal roles in chromosome dynamics. In yeast, the SMC1-SMC3 heterodimer is required for meiotic sister chromatid cohesion and DNA recombination. Little is known, however, about mammalian SMC proteins in meiotic cells. We have identified a novel SMC protein (SMC1␤), which-except for a unique, basic, DNA binding C-terminal motif-is highly homologous to SMC1 (which may now be called SMC1␣) and is not present in the yeast genome. SMC1␤ is specifically expressed in testes and coimmunoprecipitates with SMC3 from testis nuclear extracts, but not from a variety of somatic cells. This establishes for mammalian cells the concept of cell-type-and tissue-specific SMC protein isoforms. Analysis of testis sections and chromosome spreads of various stages of meiosis revealed localization of SMC1␤ along the axial elements of synaptonemal complexes in prophase I. Most SMC1␤ dissociates from the chromosome arms in late-pachytene-diplotene cells. However, SMC1␤, but not SMC1␣, remains chromatin associated at the centromeres up to metaphase II. Thus, SMC1␤ and not SMC1␣ is likely involved in maintaining cohesion between sister centromeres until anaphase II.The eukaryotic, evolutionarily highly conserved SMC (Structural Maintenance of Chromosomes) proteins are involved in several key DNA and chromatin dynamic processes (for recent reviews, see references 11, 21, 26, 27, 31, 48, 60, and 62). The best-documented processes are chromosome condensation and sister chromatid cohesion. Evidence is also accumulating for a function in DNA recombination and repair. A fourth role of SMC proteins is in gene dosage compensation in Caenorhabditis elegans. The phylogenetic tree comprises five subfamilies (32): SMC1 to SMC4 and an ancestral family that includes the recently defined SMC5 and SMC6 groups with the Rad18 and Spr18 proteins of Schizosaccharomyces pombe (16), which act in recombinational repair.SMC proteins share a characteristic design. Coiled-coil domains are flanked by globular N-and C-terminal domains and are divided in the central region by a flexible hinge domain of about 150 aa. The N-and C-terminal domains of about 100 to 150 aa are highly conserved and carry important motifs. The N-terminal domain includes an NTP binding motif (Walker A box [68]), which has been shown to bind the ATP analogue azido-ATP (1). The C-terminal domain contains a DA box (68). The C-terminal and second coiled-coil domains, but not the N terminus, bind DNA (1, 2). It has been proposed that the antiparallel, heterodimeric SMC1-SMC3 protein with an N and C terminus at each end may connect two DNA molecules, such as sister chromatids, and may directly contribute to their alignment in cohesion and to recombination between sister chromatids (2, 26, 62).In eukaryotes the SMC1-SMC3 or SMC2-SMC4 heterodimers form large multiprotein complexes. One of these complexes is condensin, which, besides the SMC2-SMC4 heterodimer, contains several non-SMC subunits. Condensin is necessary for mitotic chromosome c...

show abstract

“…To explore nonhomologous joining in vitro we have employed oocytes and eggs of Xenopus laevis, known to be a rich source of ligation and recombination activities. (22)(23)(24)(25)(26).…”

Section: Introductionmentioning

confidence: 99%

Joining of nonhomologous DNA double strand breaksin vitro

1988

View full text Add to dashboard Cite

Extracts of Xenopus laevis eggs can efficiently join ends of duplex DNA that differ in structure and sequence. This was analysed by recircularisation of linear plasmid DNA molecules with dissimilar termini, generated by successive cuts with two different restriction enzymes within the pSP65 polylinker. Use of various enzymes provided blunt ended or 4 nucleotides long 3' and 5' protruding single strand (PSS) termini which were successfully joined in vitro in any tested combination. Sequence analysis of numerous junctions from cloned reaction products of 7 terminus combinations reveal: apart from very rare base exchanges and single nucleotide insertions less than 10% deletions (1 to 18 nucleotides long) were detected. Blunt/PSS or 3'PSS/5'PSS terminus pairs undergo simple "blunt end" joining which preserves PSS ends by fill-in. In contrast, equally polar 3'PSS/3'PSS or 5'PSS/5'PSS terminus pairs are joined by a complex mode: PSS ends overlap by a defined number of nucleotides, set by matching basepairs. Even one basematch suffices to define the setting. This then determines the final mismatch repair and fill-in pattern. We propose that yet unknown terminal DNA-binding proteins stabilize the energetically highly unfavorable configuration of single matching basepairs and help to support defined overlap structures.

show abstract

DNA binding protein from ovaries of the frog, Xenopus laevis which promotes concatenation of linear DNA

Cited by 24 publications

References 23 publications

Activation of a system for the joining of nonhomologous DNA ends during Xenopus egg maturation.

Activation of a system for the joining of nonhomologous DNA ends during Xenopus egg maturation.

Novel Meiosis-Specific Isoform of Mammalian SMC1

Joining of nonhomologous DNA double strand breaksin vitro

Contact Info

Product

Resources

About