Figure 5.
Knockout of SNORD42A reduces cell size and synthesis of nascent polypeptide chains. (A) Mean diameter of SNORD42A knockout (n = 245) and control Kasumi-1 cells (n = 235) (microscope: Zeiss AxioVert.A1, objective 40×; camera: Zeiss AxiocamMRm). Data are shown as mean ± SD; ***P < .001, Student t test. (B) Forward scatter size fluorescence-activated cell sorting histogram of SNORD42A knockout and control Kasumi-1 cells. (C) Fluorescence-activated cell sorting histogram of OP incorporation in SNORD42A knockout and control Kasumi-1 cells and mean intensity of OP-Puro fluorescence in SNORD42A knockout and control Kasumi-1 cells (n = 2 measurements from independent infections). (D) Structure of the 40S ribosome indicating the SNORD42A methylation site U116 in the 40S ribosomal unit (Protein Data Bank accession number 4UG0).

Knockout of SNORD42A reduces cell size and synthesis of nascent polypeptide chains. (A) Mean diameter of SNORD42A knockout (n = 245) and control Kasumi-1 cells (n = 235) (microscope: Zeiss AxioVert.A1, objective 40×; camera: Zeiss AxiocamMRm). Data are shown as mean ± SD; ***P < .001, Student t test. (B) Forward scatter size fluorescence-activated cell sorting histogram of SNORD42A knockout and control Kasumi-1 cells. (C) Fluorescence-activated cell sorting histogram of OP incorporation in SNORD42A knockout and control Kasumi-1 cells and mean intensity of OP-Puro fluorescence in SNORD42A knockout and control Kasumi-1 cells (n = 2 measurements from independent infections). (D) Structure of the 40S ribosome indicating the SNORD42A methylation site U116 in the 40S ribosomal unit (Protein Data Bank accession number 4UG0).

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