Persistence of chromosomal proteins HMG-14/-17 in myotubes following differentiation-dependent reduction of HMG mRNA.

نویسندگان

  • J M Pash
  • J S Bhorjee
  • B M Patterson
  • M Bustin
چکیده

The expression of chromosomal proteins HMG-14 and HMG-17 during cellular differentiation was studied in cultured mouse myoblasts. During myogenesis the level of both HMG-14 and HMG-17 mRNA decreased to less than 20% of that found in myoblasts. The down-regulation of HMG-14/-17 mRNA occurred simultaneously with activation of muscle-specific actin mRNA and was not linked to DNA synthesis, indicating that it is a differentiation-, rather than a cell cycle-related event. Incorporation of radiolabeled lysine into HMG proteins was similar to that into the major histone fractions in that it was significant in myoblasts and undetectable in myotubes. The decrease in mRNA and protein synthesis did not affect the cellular levels of HMG protein. These results indicate that the regulation of HMG-14/-17 mRNA levels is different from that of the histones and is linked to differentiation rather than to DNA synthesis.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Expression of chromosomal proteins HMG-14 and HMG-17 in transformed human cells.

The relation between cellular phenotype and expression of chromosomal high mobility group proteins 14 and 17 (HMG-14 and HMG-17) has been examined in human cell lineages. Quantitation of HMG-14 and HMG-17 mRNA in several human cell lines revealed differences in both the steady state mRNA level and in the ratio of HMG-14 to HMG-17 mRNA. Analysis of phenotypically distinct derivatives of human br...

متن کامل

CHARACTERIZATION OF HIGH MOBILITY GROUP NONHISTONE PROTEINS FROM DIFFERENTIATED NEUROPHILIC GRANULOCYTES

The quantitative changes of the high mobility group (HMG) nonhistone chromosomal proteins in nondividing, differentiated peritoneal exudate neutrophils were identified by their solubility, electrophoretic mobility on both SDS and acetic acid gels, densitometric traces and elution profile on CM-sephadex. The results indicated that in neutrophils, HMGl undergoes a considerable reduction (80%...

متن کامل

SEPARATION OF NONHISTONE HIGH MOBILITY GROUP (HMG) FROM HUMAN LYMPHOCYTES BY HIGH PERFORMANCE LIQUID CHROMATOGRAPHY

The high mobility group (HMG) of nonhistone proteins have been investigated using two high performance liquid chromatographic techniques (HPLC). Reversed-phase HPLC under conditions of 50 mM triethylamine adjusted to pH 2.2 with phosphoric acid (solvent A) and 95% acetonitrile in water (solvent B) was used to separate proteins primarily on the basis of differences in the overall hydrophobi...

متن کامل

Dynamic relocation of chromosomal protein HMG-17 in the nucleus is dependent on transcriptional activity.

Chromosomal proteins HMG-14/-17 are nucleosomal binding proteins, which alter the structure of the chromatin fiber and enhance transcription, but only from chromatin templates. Here we show that in tissue culture cells, HMG-17 protein colocalizes with sites of active transcription. Incubation of permeabilized cells with a peptide corresponding to the nucleosomal binding domains of HMG-14/-17 sp...

متن کامل

Neither HMG-14a nor HMG-17 gene function is required for growth of chicken DT40 cells or maintenance of DNaseI-hypersensitive sites.

HMG-14 and HMG-17 form a family of ubiquitous non-histone chromosomal proteins and have been reported to bind preferentially to regions of active chromatin structure. Our previous studies demonstrated that the chicken HMG-17 gene is dispensable for normal growth of the DT40 chicken lymphoid cell line. Here it is shown that the major chicken HMG-14 gene,HMG-14a, is also dispensable and, moreover...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 265 8  شماره 

صفحات  -

تاریخ انتشار 1990