Your browser doesn't support javascript.
loading
Intermolecular Interactions between Cysteine and Aromatic Amino Acids with a Phenyl Moiety in the DNA-Binding Domain of Heat Shock Factor 1 Regulate Thermal Stress-Induced Trimerization.
Lee, Chang-Ju; Choi, Bo-Hee; Kim, So-Sun; Kim, David Nahm-Joon; Kim, Tae-Hwan; Choi, Jeong-Mo; Pak, Youngshang; Park, Jang-Su.
Afiliación
  • Lee CJ; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Choi BH; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Kim SS; East Sea Fisheries Research Institute, National Institute of Fisheries Science, Gangneung-si 25435, Republic of Korea.
  • Kim DN; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Kim TH; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Choi JM; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Pak Y; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
  • Park JS; Department of Chemistry and Chemistry, Institute of Functional Materials in Pusan National University, Busan 609-735, Korea.
Biochemistry ; 63(10): 1307-1321, 2024 May 21.
Article en En | MEDLINE | ID: mdl-38688031
ABSTRACT
In this study, we investigated the trimerization mechanism and structure of heat shock factor 1 (HSF1) using western blotting, tryptophan (Trp) fluorescence spectroscopy, and molecular modeling. First, we examined the DNA-binding domains of human (Homo sapiens), goldfish (Carassius auratus), and walleye pollock (Gadus chalcogrammus) HSF1s by mutating key residues (36 and 103) that are thought to directly affect trimer formation. Human, goldfish, and walleye pollock HSF1s contain cysteine at residue 36 but cysteine (C), tyrosine (Y), and phenylalanine (F), respectively, at residue 103. The optimal trimerization temperatures for the wild-type HSF1s of each species were found to be 42, 37, and 20 °C, respectively. Interestingly, a mutation experiment revealed that trimerization occurred at 42 °C when residue 103 was cysteine, at 37 °C when it was tyrosine, and at 20 °C when it was phenylalanine, regardless of the species. In addition, it was confirmed that when residue 103 of the three species was mutated to alanine, trimerization did not occur. This suggests that in addition to trimerization via disulfide bond formation between the cysteine residues in human HSF1, trimerization can also occur via the formation of a different type of bond between cysteine and aromatic ring residues such as tyrosine and phenylalanine. We also confirmed that at least one cysteine is required for the trimerization of HSF1s, regardless of its position (residue 36 or 103). Additionally, it was shown that the trimer formation temperature is related to growth and survival in fish.
Asunto(s)
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cisteína / Aminoácidos Aromáticos / Factores de Transcripción del Choque Térmico Límite: Animals / Humans Idioma: En Revista: Biochemistry Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Cisteína / Aminoácidos Aromáticos / Factores de Transcripción del Choque Térmico Límite: Animals / Humans Idioma: En Revista: Biochemistry Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos