Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein.
Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase alpha.
Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding factor SPN.
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.
The Paf1 complex physically and functionally associates with transcription elongation factors in vivo.
Yng1p modulates the activity of Sas3p as a component of the yeast NuA3 Hhistone acetyltransferase complex.
RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach.
Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT complexes and to reorganize nucleosomes.
High-definition macromolecular composition of yeast RNA-processing complexes.
Structural features of nucleosomes reorganized by yeast FACT and its HMG box component, Nhp6.
The yeast FACT complex has a role in transcriptional initiation.
A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery.
Proteome survey reveals modularity of the yeast cell machinery.
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Structural and functional analysis of the Spt16p N-terminal domain reveals overlapping roles of yFACT subunits.
FACT and the proteasome promote promoter chromatin disassembly and transcriptional initiation.
yFACT induces global accessibility of nucleosomal DNA without H2A-H2B displacement.
A global protein kinase and phosphatase interaction network in yeast.
Defining the budding yeast chromatin-associated interactome.
The Modifier of Transcription 1 (Mot1) ATPase and Spt16 Histone Chaperone Co-regulate Transcription through Preinitiation Complex Assembly and Nucleosome Organization.
FACT mediates cohesin function on chromatin.
The social and structural architecture of the yeast protein interactome.
Deep Research Report (Falcon/Edison): Saccharomyces cerevisiae SPT16 (UniProt P32558) — FACT complex subunit Spt16/Cdc68
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SPT16/Cdc68 is the large, essential subunit of the conserved yeast FACT histone chaperone; in S. cerevisiae it
forms a heterodimer with Pob3, and budding-yeast FACT function additionally depends on the HMGB protein Nhp6 for
efficient nucleosome engagement.
"Spt16 is the large, essential subunit of the conserved yeast FACT histone chaperone complex; in *S. cerevisiae* it forms a heterodimer with Pob3, and budding-yeast FACT function additionally depends on the HMGB protein Nhp6 for efficient nucleosome engagement. Spt16 is also referred to as Cdc68, matching the yeast FACT subunit identity rather than metazoan SPT16 orthologs."
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FACT is ATP-independent (lacks an intrinsic ATPase) and remodels nucleosomes through multivalent binding and
stabilization of partially unwrapped nucleosome intermediates rather than fully wrapped nucleosomes.
"A core conceptual point emphasized in recent syntheses is that FACT is **ATP-independent** (i.e., it lacks an intrinsic ATPase) and instead remodels nucleosomes through multivalent binding and stabilization of intermediate nucleosome states."
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Spt16/FACT is a nucleosome-templated transcription elongation factor required for efficient RNAPII transcription
on chromatin templates, managing both nucleosome disassembly and reassembly as polymerase traverses genes, and
suppressing cryptic initiation.
"- is required for efficient RNAPII transcription on chromatin templates and functions as a **nucleosome-templated elongation factor**, (schweighofer2025biochemicalinsightsinto pages 22-25, hou2025characterizingthefunctional pages 20-23)
- helps manage nucleosome dynamics (both **disassembly** and **reassembly**) as RNAPII traverses genes, (byrd2024assessingcontributionsof pages 1-2)
- suppresses **cryptic initiation** and supports chromatin integrity, consistent with its chaperone role maintaining proper nucleosome organization."
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Spt16 functions at replication forks: its N-terminal domain binds Tof1 (fork protection complex) and the MCM2-7
helicase, and FACT physically interacts with DNA polymerase alpha, consistent with replication-coupled parental
histone recycling and nucleosome reassembly.
"- The Spt16 N-terminal domain binds **Tof1** (fork protection complex) and **MCM2-7** helicase in yeast, linking FACT to fork-associated chromatin transactions. (schweighofer2025biochemicalinsightsintoa pages 22-25, dolson2024impactofthe pages 16-19)
- FACT is reported to physically interact with **DNA polymerase α** in yeast."
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In vivo deletion of the Spt16 N-terminal domain (spt16-deltaN) disrupts parental histone recycling and reduces
parental H3K4me3 recycling globally; cryo-EM places FACT at the front of the fork with the middle and C-terminal
modules contacting H3-H4 and H2A-H2B respectively.
"A 2024 thesis-style synthesis of replication-coupled chromatin processes cites recent in vivo findings that deletion of the Spt16 N-terminal domain (spt16ΔN) disrupts aspects of parental histone recycling and reduces parental H3K4me3 recycling globally; it also cites cryo-EM placement of FACT at the front of the fork, where Spt16’s middle and C-terminal modules contact H3–H4 and H2A–H2B, respectively, consistent with a model in which FACT helps disassemble and reassemble nucleosomes during fork progression."
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In budding yeast FACT acts primarily in euchromatin (including promoter chromatin activation of SBF/MBF-regulated
G1/S cell-cycle genes), with no clear evidence for SIR-dependent heterochromatin silencing; heterochromatin roles
seen in fission yeast (via Swi6/HP1) appear species-specific.
"- In **budding yeast**, FACT is presented primarily as acting in **euchromatin**, including promoter chromatin activation via interactions with SBF/MBF in regulation of G1/S cell cycle genes; the review notes a lack of evidence for roles in **SIR-dependent** heterochromatin silencing in budding yeast."
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Spt16 is nuclear and chromatin-associated, acting at promoters/+1 nucleosomes and transcribed gene bodies, at
replication forks (via Tof1/MCM and Pol alpha), and with reported centromeric enrichment whose specific role
remains unresolved.
"The evidence supports that Spt16 is **nuclear and chromatin-associated**, acting at:"