The fission yeast spo20+ gene encodes a glycerophospholipid‐transfer protein. spo20 mutants are unable to assemble the forespore membrane properly. Here we studied the structural integrity of the spindle pole body (SPB) in spo20‐H6 mutants during meiosis. Meiotic cells expressing a GFP‐tagged SPB marker protein, Spo15‐GFP, showed an excess number of SPBs, some of which were not localized to the spindle poles and were termed ‘pseudo‐SPBs’. Formation of spindles for meiosis I was significantly delayed in spo20‐H6 cells, although the morphology of spindles and segregation of the sister chromatids seemed normal. The SPB of spo20‐H6 contained meiosis‐specific outer plaques, though outermost layers were less evident. Time‐lapse studies of spo20‐H6 cells showed that the pseudo‐SPBs originated from normal SPBs at the spindle poles during meiosis I. Among the SPB components tested, Spo15, Spo13, Sad1 and Cut12 were localized to the pseudo‐SPBs, but Sid4 was not always present. Alp4, a component of the γ‐tubulin complex, was also present in about 40% of the pseudo‐SPBs. The forespore membranes initiated from both the SPBs and the pseudo‐SPBs. We conclude that Spo20 plays a role in maintaining the structural integrity of the meiotic SPB, besides supplying membrane vesicles for forespore membrane assembly.