Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206

Liang, Yu; Choo, Siew Hua; Roßbach, Michael; Baburajendran, Nithya; Palasingam, Paaventhan; Kolatkar, Prasanna R.

doi:10.1107/s1744309112006070

Cited by 4 publications

(7 citation statements)

References 19 publications

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“…(A) A typical domain structure of the SCAN C2H2 and SCAN KRAB C2H2 proteins. (B) The crystal structure of a SCAN domain dimer from the Zfp206 protein [ 110 ].…”

Section: Transcription Factors With a Cluster Of C2h2 Domains And An mentioning

confidence: 99%

C2H2 Zinc Finger Proteins: The Largest but Poorly Explored Family of Higher Eukaryotic Transcription Factors

et al. 2017

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The emergence of whole-genome assays has initiated numerous genome-wide studies of transcription factor localizations at genomic regulatory elements (enhancers, promoters, silencers, and insulators), as well as facilitated the uncovering of some of the key principles of chromosomal organization. However, the proteins involved in the formation and maintenance of the chromosomal architecture and the organization of regulatory domains remain insufficiently studied. This review attempts to collate the available data on the abundant but still poorly understood family of proteins with clusters of the C2H2 zinc finger domains. One of the best known proteins of this family is a well conserved protein known as CTCF, which plays a key role in the establishment of the chromosomal architecture in vertebrates. The distinctive features of C2H2 zinc finger proteins include strong and specific binding to a long and unique DNA recognition target sequence and rapid expansion within various animal taxa during evolution. The reviewed data support a proposed model according to which many of the C2H2 proteins have functions that are similar to those of the CTCF in the organization of the chromatin architecture.

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“…(A) A typical domain structure of the SCAN C2H2 and SCAN KRAB C2H2 proteins. (B) The crystal structure of a SCAN domain dimer from the Zfp206 protein [ 110 ].…”

Section: Transcription Factors With a Cluster Of C2h2 Domains And An mentioning

confidence: 99%

C2H2 Zinc Finger Proteins: The Largest but Poorly Explored Family of Higher Eukaryotic Transcription Factors

et al. 2017

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“…pDEST-HisMBP-Zfp206SCAN expression vector was constructed as described previously ( 19 ). An analogous strategy was used to generate additional SCAN domains.…”

Section: Methodsmentioning

confidence: 99%

“…The procedure for the expression and purification of Zfp206SCAN protein and other factors was carried out as described previously ( 19 ). In brief, the pDEST-HisMBP expression plasmids with different SCAN domain inserts were transformed into Escherichia coli BL21 (DE3) cells (Invitrogen).…”

Section: Methodsmentioning

confidence: 99%

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Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206

Liang

Hong

Pugalenthi

et al. 2012

Nucleic Acids Research

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Zfp206 (also named as Zscan10) belongs to the subfamily of C 2 H 2 zinc finger transcription factors, which is characterized by the N-terminal SCAN domain. The SCAN domain mediates self-association and association between the members of SCAN family transcription factors, but the structural basis and selectivity determinants for complex formation is unknown. Zfp206 is important for maintaining the pluripotency of embryonic stem cells presumably by combinatorial assembly of itself or other SCAN family members on enhancer regions. To gain insights into the folding topology and selectivity determinants for SCAN dimerization, we solved the 1.85 Å crystal structure of the SCAN domain of Zfp206. In vitro binding studies using a panel of 20 SCAN proteins indicate that the SCAN domain Zfp206 can selectively associate with other members of SCAN family transcription factors. Deletion mutations showed that the N-terminal helix 1 is critical for heterodimerization. Double mutations and multiple mutations based on the Zfp206SCAN–Zfp110SCAN model suggested that domain swapped topology is a possible preference for Zfp206SCAN–Zfp110SCAN heterodimer. Together, we demonstrate that the Zfp206SCAN constitutes a protein module that enables C 2 H 2 transcription factor dimerization in a highly selective manner using a domain-swapped interface architecture and identify novel partners for Zfp206 during embryonal development.

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“…Zscan10 consists of 6 exons and encodes the protein containing 782 amino acids [12,13]. into EB5 ES cells (Fig.1).…”

Section: Generation Of Inducible Knockout Es Cells Of Zscan10mentioning

confidence: 99%

Zscan10 is dispensable for maintenance of pluripotency in mouse embryonic stem cells

Yamane¹,

Fujii²,

Ohtsuka³

et al. 2015

Biochemical and Biophysical Research Communications

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Zinc finger and SCAN domain-containing 10 (Zscan10, also known as Zfp206) encodes a transcription factor that has been reported to be involved in the maintenance of pluripotency in mouse embryonic stem (ES) cells. Here we generated inducible knockout ES cells for Zscan10 using the Cre-loxP system and analyzed its function. We succeeded in establishing Zscan10-null ES cells and confirmed their pluripotency by the generation of chimeric embryos. Our results clearly indicate that Zscan10 is dispensable for the ability of self-renewal and differentiation in ES cells.

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Crystal optimization and preliminary diffraction data analysis of the SCAN domain of Zfp206

Cited by 4 publications

References 19 publications

C2H2 Zinc Finger Proteins: The Largest but Poorly Explored Family of Higher Eukaryotic Transcription Factors

C2H2 Zinc Finger Proteins: The Largest but Poorly Explored Family of Higher Eukaryotic Transcription Factors

Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206

Zscan10 is dispensable for maintenance of pluripotency in mouse embryonic stem cells

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