2003
DOI: 10.1016/j.bbrc.2003.09.235
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Molecular cloning of a novel human gene encoding histone acetyltransferase-like protein involved in transcriptional activation of hTERT

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Cited by 64 publications
(51 citation statements)
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“…S3A). These data indicated increased binding of cluster b proteins to heterochromatin in response to hypoxia stress, consistent with a role for these molecules in the repression of tumor suppressor genes during malignant progression (35,36). In agreement with our proteomic data, other investigators have recently reported a role for KDM5B in regulating the expression of E2f genes via remodeling of heterochromatin during cell cycle progression (37), and our Western blot analysis confirmed that HP1BP3 binding to chromatin was increased by hypoxia stress (supplemental Figs.…”
Section: Resultssupporting
confidence: 56%
“…S3A). These data indicated increased binding of cluster b proteins to heterochromatin in response to hypoxia stress, consistent with a role for these molecules in the repression of tumor suppressor genes during malignant progression (35,36). In agreement with our proteomic data, other investigators have recently reported a role for KDM5B in regulating the expression of E2f genes via remodeling of heterochromatin during cell cycle progression (37), and our Western blot analysis confirmed that HP1BP3 binding to chromatin was increased by hypoxia stress (supplemental Figs.…”
Section: Resultssupporting
confidence: 56%
“…Human NAT10 (also known as hALP) was initially identified as a transcriptional factor that interacts with the promoter region of hTERT (telomerase reverse transcriptase) (45). Recombinant NAT10/hALP (amino acids 164 -834) lacking the N-terminal domains had an ability to acetylate calf thymus histones in vitro in the presence of acetyl-CoA (without ATP), indicating that NAT10/hALP has a histone acetyltransferase activity that might promote hTERT transcription via decondensation of chromatin structure (45).…”
Section: Discussionmentioning
confidence: 99%
“…Human NAT10 (also known as hALP) was initially identified as a transcriptional factor that interacts with the promoter region of hTERT (telomerase reverse transcriptase) (45). Recombinant NAT10/hALP (amino acids 164 -834) lacking the N-terminal domains had an ability to acetylate calf thymus histones in vitro in the presence of acetyl-CoA (without ATP), indicating that NAT10/hALP has a histone acetyltransferase activity that might promote hTERT transcription via decondensation of chromatin structure (45). However, based on the crystal structure of TmcA, the N-terminal domain of the recombinant NAT10/hALP that was missing from that construct contains a functionally important region (DUF1726) that constitutes the RNA helicase/ATPase domain required for the tRNA acetyltransferase activity (28,46).…”
Section: Discussionmentioning
confidence: 99%
“…To ask which HAT contributes this activity, we reasoned that such a HAT must be a nuclear membrane-associated moiety. An in silico search revealed that the human genome encodes a minimum of sixteen HATs (40, 41); however, only one, KIAA1709/hALP (41), is a nuclear membrane-associated protein (5).…”
Section: Determinants Of Hssun1 Localization To the Nuclearmentioning
confidence: 99%